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
|
|---|---|---|---|---|---|---|
P10058
|
HBB_EUDCH
|
Hemoglobin beta chain
|
Eudyptes
|
VHWSAEEKQLITGLWGKVNVAQCGGEALARLLIVYPWTQRFFSSFGNLSSPSAILGNPMVRAHGKKVLTSFGDAVKNMDNIKNTFAQLSELHCDKLHVDPENFRLLGDILIIVLAAHFAKDFTPECQAAWEKLVRVVAHALARKYH
|
Involved in oxygen transport from the lung to the various peripheral tissues.
|
P10058
|
A1JJF4
|
RSMA_YERE8
|
S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase
|
Yersinia
|
MNNRVHQGHFARKRFGQNFLNDQFVIDSIVSAIHPVPGEAVVEIGPGLGALTEPVAARMDHMTVIELDRDLADRLASHPQLKDKLTIHQEDAMKINFSELAELAGQPLRVFGNLPYNISTPLMFHLFSYTSAIRDMHFMLQKEVVNRLVAGPNSKAYGRLTVMAQYYCNVIPVLEVPPTAFTPAPKVDSAVVRLIPHVNTPNPVGDVRMLSRITTQAFNQRRKTVRNSLGDLFTPEQLIELGIDPILRAENISVAQYCKLANWLSAQSTPQE
|
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.
|
A1JJF4
|
A8G1W5
|
ATPB_SHESH
|
F-ATPase subunit beta
|
Shewanella
|
MSTGTVVQVIGAVVDVEFPHDAVPQVYDALEIKSEGLVLEVQQQLGGGVVRTIAMGSSDGLRRGLEVVNSGSPITVPVGEKTLGRIMNVLGEPVDEAGPIGEEDRYVIHREAPSYEDQSSSTELLETGIKVIDLVCPFAKGGKVGLFGGAGVGKTVNMMELINNIAKAHSGLSVFAGVGERTREGNDFYYEMEDSGVLDKVAMVYGQMNEPPGNRLRVALTGLTMAEKFRDEGKDVLFFVDNIYRYTLAGTEVSALLGRMPSAVGYQPTLAEEMGVLQERITSTKTGSITSVQAVYVPADDLTDPSPATTFAHLDATVVLSRNIASLGIYPAVDPLDSTSRQLDPQVVGQEHYDVATGVQTQLQRYKELKDIIAILGMDELSDDDKTTVFRARKIEKYLSQPFFVAEVFTGSPGKYVSLKDTIRGFKGILDGEFDHLPEQAFYMVGSIDEAVEKANKK
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
|
A8G1W5
|
Q5L0S3
|
FMT_GEOKA
|
Methionyl-tRNA formyltransferase
|
Geobacillus thermoleovorans group
|
MTNIVFMGTPDFAVPILRQLLDDGYHVAAVVTQPDKPKGRKREPVPPPVKVEAERRGIPVLQPTKIREPEQYEQVLAFAPDLIVTAAFGQILPKALLDAPKYGCINVHASLLPELRGGAPIHYAIWQGKTKTGVTIMYMVERLDAGDMLAQVEVPIAETDTVGTLHDKLSAAGAKLLSETLPLLLEGNIAPVPQDEEKATYAPNIRREQERIDWTQPGEAIYNHIRAFHPWPVTYTTQDGHIWKVWWGEKVPAPRSAPPGTILALEENGIVVATGNETAIRITELQPAGKKRMAVGEFLRGAGSRLAVGMKLGEDHERT
|
Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
|
Q5L0S3
|
Q09X07
|
PSAI_MORIN
|
Photosystem I reaction center subunit VIII
|
Morus
|
MTTISNLPAIFVPLVGLVFPAIAMVSLSLHVQKNKIF
|
May help in the organization of the PsaL subunit.
|
Q09X07
|
Q46TH1
|
FLHC_CUPPJ
|
Flagellar transcriptional regulator FlhC
|
Cupriavidus
|
MKTTAQTAPARSALQDASDTQLAIELIGLGARPQVVEAEVTLSRSRVYRLYRELTGGSPPKGMLPFSADWFVTWRPNAHASYLLSVHEYMQQRAGLPGIRAVLNSYRVYAEHMKANNEECLISFTRFWTLVRFCEGGLLQLSTCPCCGGRFVTHAHEPLASFICTLCQPPSRVRRSVRRETPHATANAPAAVLGNRPPVAMPGFGMVPAL
|
Functions in complex with FlhD as a master transcriptional regulator that regulates transcription of several flagellar and non-flagellar operons by binding to their promoter region. Activates expression of class 2 flagellar genes, including fliA, which is a flagellum-specific sigma factor that turns on the class 3 genes. Also regulates genes whose products function in a variety of physiological pathways.
|
Q46TH1
|
Q487K8
|
NAGB_COLP3
|
Glucosamine-6-phosphate isomerase
|
Colwellia
|
MQVIIFDNAQQVAENAAEWVAELINKKSNPVLGLATGSTPISLYQELVNKYKAGELSFSNTTSFNLDEYLGINEKNQQSYRHFMNENLFNHVDINKLKTFLPTCNQGENPREQGLDYEDKIAQAGGIDLQILGIGANGHIGFNEPTSSLASRTRIKTLTQQTLNDNSRLFAADEFQPTLAMTMGIATILDARYVLLMATGKSKAKAVKEMVTGPLSAVCPASSLQLHENAIVLLDKEAASELEDHEYYVWADKQNVKINQEFGLYHNY
|
Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
|
Q487K8
|
Q5B7I7
|
INPE_EMENI
|
Inp cluster protein E
|
Aspergillus subgen. Nidulantes
|
MAKETRFYPYTSNGGATLGVSGPDFAILAGDTRSTAGYNINTRYEPKVFTIQDARDRSIVISVIGFAADGRALKERLDAIVAMYKYQHGKNIGLRACAQRVSTMLYEKRFFPYQLQTMVAGIDADGQGAIYYYDPAGCIEKRSHCAAGEASSLMLPFLDSQAPRLQPLSLQTAQQLVRDAYTGATERHIEVGDHLQMLVVTREGVSEQLVDLKKD
|
Proteasome subunit beta type-6; part of the inp gene cluster that mediates the biosynthesis of fellutamide B, a mycotoxin that acts as a proteasome inhibitor . In the first step of fellutabmide B biosynthesis inpC activates 3-hydroxydodecanoic acid to generate 3-hydroxydodecanoyl-AMP that is then loaded onto the T0 domain of inpB . The 3-hydroxydodecanoyl-S-phosphopantetheinyl-T0 is sequentially extended with L-Asn and L-Gln by the two CAT modules of inpB . The linear lipodipeptide from inpB is then transferred onto inpA for the addition of the third amino acid, L-Leu . Reductive releasing of the lipotripeptide by the TE domain of inpA produces (2S)-fellutamide B . InpF might be involved in the release and transfer of the lipodipeptide from inpB to inpA . The inp cluster-encoded proteasome subunit inpE confers resistance to internally produced fellutamides . The MFS efflux transporter inpD may contribute to fellutamide resistance as well .
|
Q5B7I7
|
Q0BTX6
|
PYRG_GRABC
|
UTP--ammonia ligase
|
Granulibacter
|
MTRFVFITGGVVSSLGKGIASAALGALLQARGYSVRLRKLDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFTGVHARKSDNATTGRIYSDVIARERRGDYLGATVQVIPHITDAIKDAVTRDLNQDLDFALIEIGGTVGDIESLPFLEAIRQLGNELGPSRTMFVHLTLVPYIPSAGELKTKPTQHSVKELQNVGIQPNMLLCRCDRLIPENERRKIANFCNVRQEAVVSALDVDTIYSVPIRYHEEGMDREVLRHFNLPIGGEPDLTRWREIADVVRAPDGVVKIAIVGKYITLLDSYKSLAEALVHGGIANRVKVEIDWVDSQIFEQADSVQRLEGVHGILVPGGFGERGAEGKIEAVRFAREHKVPFLGICFGMQMAVIEAARNLAGLPDASSTEFGPCEVPIVGLMTEWARGNDLERRSASGDLGGTMRLGSYPAALIEGSLARETYGGVPVVQERHRHRYEVNIHYREQLEAVGLRFSGLSPDGVLPEIVEYADHPWFVGVQYHPELKSKPFDPHPLFSGFVAAAVRQARLV
|
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.
|
Q0BTX6
|
Q2Y791
|
RL31_NITMU
|
50S ribosomal protein L31
|
Nitrosospira
|
MKPDIHPDYQEITVTCSCGSTFQTRSTMGKPLHIEVCSVCHPFYTGKQKIVDTAGRVEKFRQKYGKKVEKQPAAG
|
Binds the 23S rRNA.
|
Q2Y791
|
A9NB52
|
RNH_COXBR
|
Ribonuclease H
|
Coxiella
|
MAKQEQNIVYLYCDGACRGNPGPGGWGVLLRYNQHERQLHGGVANTTNNQMELTAAIEGLKSLKKPCQVVVTTDSQYLRRGITEWLPVWKRRGWRTSNKKPVKNQPLWETLEREVERHTIVWHWVKGHSGHAENEIADELANRGIDEVLKRGVQ
|
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
|
A9NB52
|
A2RD01
|
IF2_STRPG
|
Translation initiation factor IF-2
|
Streptococcus
|
MSKKRLHEIAKEIGKSSKEVVEHAKYLGLDVKSHASSVEEADAKKIISSFSKASKPDVTASQAVKPKEVAQPSVTVVKETGSEHVEKTQVSKPKSRNFKAEREARAKEQAARKQANGSSHRSQERRGGYRQPNNHQTNEQGDKRITHRSQGDTNDKRIERKASNVSPRHDNHQLVGDRNRSFAKENHKNGRFTNQKKQGRQEPQSKSPKIDFKARAAALKAEQNAEYSRQSETRFRAQQEAKRLAELARQEAKEAALKAQAEEMSHREAALKSIEEAETKLKSSNISAKSTADNRRKKQARPEKNRELTHHSQEGQKKNKKSWNSQNQVRNQKNSNWNKNKKTKKGKNVKNTNTAPKPVTERKFHELPKEFEYTEGMTVAEIAKRIKREPAEIVKKLFMMGVMATQNQSLDGDTIELLMVDYGIEAKAKVEVDDADIERFFEDENYLNPENIVERAPVVTIMGHVDHGKTTLLDTLRNSRVATGEAGGITQHIGAYQIEEAGKKITFLDTPGHAAFTSMRARGASVTDITILIVAADDGVMPQTIEAINHSKAAGVPIIVAINKIDKPGANPERVIAELAEYGIISTAWGGECEFVEISAKFNKNIDELLETVLLVAEVEELKADPTVRAIGTVIEARLDKGKGAIATLLVQQGTLHVQDPIVVGNTFGRVRAMVNDLGRRVKSAEPSTPVSITGLNETPMAGDHFAVYADEKAARAAGEERSKRALLKQRQNTQRVSLDNLFDTLKAGEIKTVNVIIKADVQGSVEALAASLVKIEVEGVRVNVVHSAVGAINESDVTLAEASNAVIIGFNVRPTPQARQQADTDDVEIRLHSIIYKVIEEVEEAMKGKLDPVYQEKVLGEAIIRETFKVSKVGTIGGFMVINGKVTRDSSVRVIRDSVVIFDGKLASLKHYKDDVKEVGNAQEGGLMIENFNDLKVDDTIEAYIMEEIVRK
|
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
|
A2RD01
|
A3MXH2
|
COXX1_PYRCJ
|
Heme O synthase 1
|
Pyrobaculum
|
MKAYLTLLKPRVIWLLILASAAGYVYAAGGVDWGKLSSLLLAALLATGGSAAFNHYWERDIDAAMRRTSRRPLPMGLIKPGRALAFSLALSAAGVALGFLLLGPLPGAFVALGWFFYAVVYTMWLKRRSWLNVLAGGFAGNAVFLGGYALGKGHIDLAAVLMSFAVYLWIPAHIWSLAYKYKEDYRRAGVPMLPVVIGEQKAVVVISVLNVASVAYIALLTLLFLPSLLSLLLVAVGAGAAVASSIYALVKRTEGAMWKMYKSSAPVLTIFLVAVMLA
|
Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
|
A3MXH2
|
Q2VZ23
|
RL25_MAGSA
|
General stress protein CTC
|
Magnetospirillum
|
MSEAIAIAAELRDGSGKGAARATRRAGKVPGVIYGDKKAAICIQMDPRVVWAQISKTGFFTQLFNVDLGKDGKHLCLARDVQMHPVTDQPIHVDFMRVSADHAIHVKVPVHFTNELKSPGIKKGGVLNVELHEIEITCSPNDIPHEILIDLDGLEIGASIHLSDLKLPAGAKPYHVASGATVASIAAPTVARAETTETEAAG
|
This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance.
|
Q2VZ23
|
Q3ITQ5
|
AMZA_NATPD
|
Archaemetzincin
|
Natronomonas
|
MHVDIVPVGDLPAVVKREASSGLRSVYDCEVTIHDSQPVPDGAYDSGRDQYRAEEFIELASRVGNGEKNIAITDTDLYYRRRNYVFGLAYLSGKGSVISTHRLQTSSDGGFSEKSAGDIFADRVRKEVVHEVGHTLGLEHCDNSRCVMNFSPTVREVDVKEENLCGSCQRQIL
|
Probable zinc metalloprotease whose natural substrate is unknown.
|
Q3ITQ5
|
Q97W44
|
PANB_SACS2
|
Ketopantoate hydroxymethyltransferase
|
Saccharolobus
|
MKKVTIRDFIKKKSMKEKITMLTAYDYPTAKIISNTTLDSILVGDSLGMVVLGYTNTLNVTMRDMISHTRAVARANPPQLIVSDMPFLSYEIDVKSAVKNAGLLVKAGSDAVKLEGGEEIKDIIRAIVKAGIPVMGHIGLTPQRFLRLGGFRTIGKTKQEEEQLIKDSLELEDAGVFSIVIENTYVDIAKRITEKLNVPTICIGAGPYCDGQVLVIHDLLGLSEVTPYFAKSYVNLKEIISSAINQYIIDVKTNKFPEKQHYKERES
|
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
|
Q97W44
|
Q3BYI0
|
GLGB2_XANC5
|
Glycogen branching enzyme 2
|
Xanthomonas
|
MSERQGGQEQRTEADGMTTEGISETSQTLQALANGLPADAFAVLGPKPLAEGRRQVRVLAPGAEAMGLIDPRGKLLARMQASAIDGVFEGILAADGPYRLRIVWPDRVQEVEDPYAFAATLDESLLLQIAAGDGQAVRRALGAQHVHCGDVPGVRFAVWAPHAQRVAVVGDFNGWDVRRHPMRQRIGGFWELFLPRVEAGARYKYAVTAADGRVLLKADPVARQTELPPATASVVPSAAAFAWTDAAWMANRDPGAVPAPLSIYEVHAASWRRDGHNQPLDWPTLAEQLIPYVQQLGFTHIELLPITEHPFGGSWGYQPLGLYAPTARHGSPDGFAQFVDACHRAGIGVILDWVSAHFPDDAHGLAQFDGAALYEHADPREGMHRDWNTLIYNYGRPEVTAYLLGSALEWIEHYHLDGLRVDAVASMLYRDYGRAEGEWVPNAHGGRENLEAVAFLRQLNREIATQFPGVLTIAEESTAWPGVTAAISDGGLGFTHKWNMGWMHDTLGYMQRDPAERAQHHSQLTFGLVYAFDERFVLPLSHDEVVHGTGGLLGQMPGDDWRRFANLRAYLALMWAHPGDKLLFMGAEFGQWADWNHDQSLDWHLLDGARHRGMQQLVGDLNAALRRTPALYRGSHRADGFDWSVADDARNSVLAFVRHDPAGGAPLLAVSNLTPQPHHDYHVGVPRAGLWREILNTDSAHYGGSNLGNSGRLATEPVGMHGHAQRLRLTLPPLATIYLQAEK
|
Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
|
Q3BYI0
|
Q5RF02
|
TCPE_PONAB
|
CCT-epsilon
|
Pongo
|
MASMGTLAFDEYGRPFLIIKDQDRKSRLMGLEALKSHIMAAKAVANTMRTSLGPNGLDKMMVDKDGDVTVTNDGATILSMMDVDHQIAKLMVELSKSQDDEIGDGTTGVVVLAGALLEEAEQLLDRGIHPIRIADGYEQAARVAIEHLDKISDSVLVDIKDTEPLIQTAKTTLGSKVVNSCHRQMAEIAVNAVLTVADMERRDVDFELIKVEGKVGGRLEDTKLIKGVIVDKDFSHPRMPKKVEDAKIAILTCPFEPPKPKTKHKLDVTSVEDYKALQKYEKEKFEEMIQQIKETGANLAICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATGGRIVPRFSELTAEKLGFAGLVQEISFGTTKDKMLVIEQCKNSRAVTIFIRGGNKMIIEEAKRSLHDALCVIRNLIRDNRVVYGGGAAETSCALAVSQEADKCPTLEQYAMRAFADALEVIPMALSENSGMNPIQTMTEVRARQVKEMNPALGIDCLHKGTNDMKQQHVIETLIGKKQQISLATQMVRMILKIDDIRKPGESEE
|
Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.
|
Q5RF02
|
Q43385
|
DOF37_ARATH
|
Transcription factor BBFa
|
Arabidopsis
|
MDATKWTQGFQEMINVKPMEQMISSTNNNTPQQQPTFIATNTRPNATASNGGSGGNTNNTATMETRKARPQEKVNCPRCNSTNTKFCYYNNYSLTQPRYFCKGCRRYWTEGGSLRNVPVGGSSRKNKRSSTPLASPSNPKLPDLNPPILFSSQIPNKSNKDLNLLSFPVMQDHHHHALELLRSNGVSSRGMNTFLPGQMMDSNSVLYSSLGFPTMPDYKQSNNNLSFSIDHHQGIGHNTINSNQRAQDNNDDMNGASRVLFPFSDMKELSSTTQEKSHGNNTYWNGMFSNTGGSSW
|
Transcription factor specifically involved in the maternal control of seed germination. Regulates transcription by binding to a 5'-AA[AG]G-3' consensus core sequence. May ensure the inactivity of a component that would be activated to trigger germination as a consequence of red light perception.
|
Q43385
|
Q68W78
|
RL3_RICTY
|
50S ribosomal protein L3
|
typhus group
|
MRTGIIAQKIGMTSVFNDKGERISLTLVKVDGCQVVGHKTLAKHGYNALVIGVKDQKISRVTKPMKQVFANAKISPKTKLKEFRISEDNFIDIASILEVDHFSVGQFVDITATTIGKGFAGSMKRHNFRGLEASHGVSISHRSHGSTGQRQDPGKVFKGKKMAGHMGCNQVTIQNLKIFAIDTNRKLIMIQGSIPGHKNSYLLVKDAIKKASITI
|
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.
|
Q68W78
|
A9BUG7
|
RUVA_DELAS
|
Holliday junction ATP-dependent DNA helicase RuvA
|
Delftia
|
MIGKLTGTLLEKNPPEVLVDCGGVGYEVQVPMSTFYNLPASGAKVSLLTHFVVREDAQLLYGFGTHSERQAFRELIKITGIGPRMALSVLSGMSVEDLAQAVTLQEVGRLVKVPGIGKKTAERLLLELKGKIGADTGAQSLFVNNDQNDIVQALMALGYSDKDAAAALKKLPPDVGVTEGIKLALKALAK
|
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.
|
A9BUG7
|
Q0HX53
|
DER_SHESR
|
GTP-binding protein EngA
|
Shewanella
|
MIPVVALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKYGRAFLSGYEFIVVDTGGIDGTEEGIETKMAEQSLAAIEEADVVLFMTDARAGLTAADLSIAQHLRSRQKTTFVVANKIDGIDADSACAEFWSLGLGEVYQMAAAQGRGVTNMIEYALTPYAEAMGIERQGEEEEVDERQYTEEEAEAEQKRLQDLPIKLAIIGKPNVGKSTLTNRILGEERVVVYDEPGTTRDSIYIPMERDGREYVIIDTAGVRRRSKVHEVIEKFSVIKTLKAVEDANVVLLIIDAREGVAEQDLGLLGFALNAGRALVIAVNKWDGIDQGIKDRVKSELDRRLGFIDFARIHFISALHGTGVGHLFESIEEAYDSATRRVSTSMLTRIMQMSQDDHQPPLVNGRRVKLKYAHAGGYNPPIVVIHGNQVSKLPDSYKRYMMNYFRRSLKVVGTPIQLRFQEGDNPFENKVEKLTMSQERRRKRALSHIKDRKTK
|
GTPase that plays an essential role in the late steps of ribosome biogenesis.
|
Q0HX53
|
A3MBD3
|
GCH4_BURM7
|
GTP cyclohydrolase FolE2
|
pseudomallei group
|
MNLMNPEFAMPDVQSTVDTRQMPIQRVGVRAVRHPLTVRTAEGETQATVGTWNLDVHLPADQKGTHMSRFVALLEERGGPLTADAFRTMLATMLEKLEARAGRIEVSFPYFVNKTAPVSGVRSLLDYEVTLTGDVRDGLTRVFAKVLVPVTSLCPCSKKISQYGAHNQRSHVTIDAELAADVPVEDLIRIAEEEASCELWGLLKRPDEKFVTERAYENPKFVEDLVRDVARRLDADERIVAYVLEAENFESIHNHSAYALIERDKRRGA
|
Converts GTP to 7,8-dihydroneopterin triphosphate.
|
A3MBD3
|
Q9W2E1
|
STUM_DROME
|
Protein stum
|
Sophophora
|
MQQTLSYSSSSPSPSPMPMPSASAAQTPPPNPNLTPNLNIRPSTNPIPRPRSTGGESAFQPAIIPVDYSYRTHTTRSILSAQSMAPSTFASNQSFVRQPSESDAQPYSSLFGDPVPPPLQPDDYFGTAAFETLRNGSVELPSSEEDALVAAMALNALIPAARERIFPSVPYSRTPRGSLLPYLQPPDIQILPNSSGGSSSEQLGSPNYRLLAPDDILNKPDVYDLENEVEEYTVVGQRMSFDDEEDEPTRTPSQAPAKLSVSSITTEDHRGLLSDSYSGRDWFRPAPQHFPEFTRIPRLRPSSKMIMSMKQDEGPLSPLATMIQDMNSSSSGGEERVAPNQSRPVSRDVVLSPKQYLEEQLGLERGSQRQSLEDYRMPPPPADPPPFRRTDLTEQDDSRSVEPEHSLKREMSPVIIRDSIPMGGDYRVEQPRPHKKTAFTILSTGQAASSAPRPPQQAPTRGRHASIQSTSTTTSSPAGRPQISPRRRSIFGSEPRLPELPSALGYTSHLVHQTTDDSPRPSVQFNMSGRHSRSKLAIPQKGILQQRDSLTSSIDTFTPRAQIRRGSIGRDPIRSLPYGQKIKSMETLPLINDQHRSSIPRLHYGSTMDLSRPEPAVFPPGALPRPLKPNLNPTRRQRGLLKIINKEESLTHNPPRSNWCSLDDLSRPSFDGTPNQARRRSSSTSPERRSSTQTVSDRRSSNLSSVTATTSDFSFRRPTLSTLPAAQTLSRMRRKSVQALSPNRIPNRIPSFGQRRQSIYQRDQEPKPLSRHGKIAKPSTLSPIIGTPNKDSSSAQSPNHRSSLMADAVDTPSEVSTRRDSVSRIPVRKSPDSRSSSPPKDFGIPASGRSSRASITRSPSRTMNAGSRSPSRSMHPSRTSSRESGRPGDSRSASRGPPSRPGSRLDQIGSRMDRPNSRLERSSSRAERSSSRADRPSSRFDVSNSRGNSRANSRLSINSSSLRSSSISPATMARNRSMRATTPSRRKSISLSPASAMMGRRKSISPDAVGQNRRVSSRGKPEPPEILSRRNSRSRIPTRSTKVASKSPPSSSKKRSKSPEKPKAMGSTPKSNKVGKGVTAKGSPKAKPKIAASAKPKTKTESLMKPPVKNANKTPVNGRPTTNAKKPASKAISTKDAKVEKGKETGKSVASKSNGKETESSVKSSKSQVTKTKPPGGTTSEAKKPATTKTHGITLEKGTNGTDPVGGIPPLAAQVGNAVLQAVEAVPAVTSEVTVPSTPGGKGAGGANMSKLVRMSSRMSLLSNKSTKVRSDSPQNRKVATVQEHATEKEETVGASSQPMSNDAAAILEKSQKTLENIQKTVTEATDEIHKTISENLTDLKSLENDLAADPSPTPSSGTTMARPGESASRTGTADGSIAPQSSGELPKSPFPPTQPIEASVSVLHPNESSAERIASVPEVECESSDLPTALDASESELVGNVMPTPESGADFKVDAKRRSPDGQGGSTAGSGGLAKSSSQEFLEDKDNVKKGGLCGCCSKLFMPCRRSRCSRCCRRRERNESAEDQPVLWSGNSSATTATNVQVIDETKPKRKKISDWLKSSCCRSCRKKPAIEEHEAHQEEVSKRTNQAANMSTGPRTRGKCGLCLSKVFCCRSVNRVDPTTGDETEMKQCCFCIPCRRGSRPNKKGSTVSWRDQDPELGIKPTESSVVEGASEAAMSAATDAGNDQVKEGCCKRFWLMLLCCRKRKRRESNARRQSIRAPPPSEDTRKKLHVDLVEYSSKMKGAIPVLPLYLAWFCAFCNVVFPGLGTLLSGLFCLCVGIPRFSQFDSARARIGSFIINIIVAVSQFFCVLFCFVGWGWSIWWGTIMLRCAKKLSKIKKVERLELEEEQRQAQLAEAGKNGVAEADKT
|
Required for locomotion and mechanical sensing in proprioceptive neurons by transducing dendrite stretching into cellular responses. Required for transduction of mechanical stimuli in a specific subpopulation of proprioceptive neurons that sense joint angles. Probably does not constitute the mechanically activated channel and may rather serve as an accessory module required for the proper localization or function of the transduction channels.
|
Q9W2E1
|
Q5P8J4
|
ILVD1_AROAE
|
Dihydroxy-acid dehydratase 1
|
Aromatoleum
|
MSDPTRPARIDERSRNVTEGVMRAPNRSMYYAMGYRETDFGKPMVGVASAHSTITPCNSGLQPLADTVAAALKEAGANPQLFGTPTVSDGIGMGTEGMKYSLVSREVIADSIETCVNGLWQDGVVVIGGCDKNMPGGMMALVRTNVPGIYVYGGTIKPGHYKGRDLNIVSVFEAVGEFIAGQLDPVDFKEIEKRACPGSGSCGGMYTANTMSAAFEALGMSLPYSSTMANEDAEKLASAAESARVLVEAIKRGLRPRDIVTREAIENAVSVIMATGGSTNAVLHFLAIAHAAEVPWTIDDFERIRRRVPVIVDMKPSGRYLATDLHQAGGIPQVMKLLLDAGLLHGACVTITGQTIAEVLENVPAAPRADQGVIRTLSDPLYAEGHLAILRGNLSPEGCVAKISGLKNPAITGPARVFDSEDDAMAAIMARRIVEGDVVVIRYEGPKGGPGMREMLAPTSALVGQGLGESVGLITDGRFSGGTWGMVVGHVSPEAFVGGPIALVREGDSVTIDAHRQLVQLNVGDEELARRAADWTPPSPRYTRGVLAKFAKFASSASKGAVTDLDL
|
Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
|
Q5P8J4
|
A7INB6
|
ENO_XANP2
|
2-phosphoglycerate dehydratase
|
Xanthobacter
|
MTAIVDIIGREILDSRGNPTVEVDVVLEDGALGRAAVPSGASTGAHEAVELRDGDASRYLGKGVGMAVDAVNGEIFDAIGGYEAEDQAHIDAALLALDGTPNKGRLGANAILGVSLAVAKAAAESKGLPLYRYVGGVNARVLPVPMMNIINGGAHADNPIDFQEFMILPAGAPSFAEGLRWGAEIFHTLKKGLKDAGHNTNVGDEGGFAPNLASAEAALEFVLKAIEKAGFKPGEDVYLGLDCASTEFFKNGVYNYEGEGTVRDIEAQVAYLAELVAKYPIVTIEDGMAEDDWVGWKLLTDTVGSKCQLVGDDLFVTNVERLSRGIKDGVGNSILVKVNQIGSLTETLDAVEMAHKAGYRAVMSHRSGETEDATIADLAVATNCGQIKTGSLARSDRTAKYNQLLRIEQELGDSARYAGKAALKALA
|
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
|
A7INB6
|
A8M8Q8
|
LYSZ_CALMQ
|
Putative [LysW]-aminoadipate/[LysW]-glutamate kinase
|
Caldivirga
|
MILVKLGGSVICGGGLDNVTNDVEPGTVLIHGGGCMVNSVMERMGVKPVILKHPNGYTSRYTDEETLKAYVMTMMLINKLIVSKLNARGIRAIGLSGVDLGLVTAKRKERVMIIDERGRTRVIDGGFSGRVTGVNVNIMNLMLSNSDVVVVSPIALSQEGLMLNVDGDQIAENIAISMNVKELVILTNVDGVLVNGKPIDKVTKANAQEILQYTTGGMRRKLETALKLTELGVRTIIANGLRDKPIRSALNGLGTVVE
|
Involved in both the arginine and lysine biosynthetic pathways. Phosphorylates the LysW-bound precursors glutamate (for arginine biosynthesis), respectively alpha-aminoadipate (for lysine biosynthesis).
|
A8M8Q8
|
C5C5S1
|
SYDND_BEUC1
|
Non-discriminating aspartyl-tRNA synthetase
|
Beutenbergia
|
MLRTSPAGSLRAEHTAQVVTLTGWVDRRRDHGGVAFIDLRDASGIAQVVIRDEAVAHPLRNEFVLQVTGEVSRRPAGNENPNLPTGEIEVVASDVVVLNSAAALPFQVSTALADTEAIGEEVRLKYRYLDLRRPAPARAIRLRAKANQAARRVLDAEEFVEIETPTLTRSTPEGARDFLVPARLAPGSWYALPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQPEFTQLDVEMSFVEQDDVIALAEKVLVALWELIGFTIPTPIPRMTFDDAMRLYGTDKPDLRFGNPIVELTSYFADTPFRVFQSEYVGAVVMAGGASLPRRQFDAWQEWAKQRGARGLAYVTFPEDGSDLGGPVAKNLSDAERAGLREATGAAPGDAVFFAAGATTPSRALLGAARQEIAKRTGLIDSADQEGAWAFVWVVDAPLFKPTGDAADDGDVALGHSAWTAVHHAFTSPTPEWIDTFEQDPGSALSNAYDIVCNGNEIGGGSIRIHRRDVQERVFQVMGIDAAEAQEKFGFLLDAFSYGAPPHGGIAFGWDRILALLTGSESIREVIAFPKSGGGYDPLTQAPAPITAEQRRESGVDAVPDDETAPQA
|
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
|
C5C5S1
|
Q8SRW9
|
SC61G_ENCCU
|
Probable protein transport protein Sec61 subunit gamma
|
Encephalitozoon
|
MSQKLQKPSFLSEYLRSIRLFSKKCVRPSGKELSMSIKRHAIGIGFLGILGYAIKLIHIPINNIIVSSPGKE
|
Necessary for protein translocation in the endoplasmic reticulum.
|
Q8SRW9
|
Q890J0
|
GLGC_LACPL
|
ADP-glucose synthase
|
Lactiplantibacillus
|
MQDEMLGIILAGGQGTRLGKLTKDTAKPAVPFGGRYRIIDFTLSNCANSGVNTVGVITQYQPLELNAHIGSGASWGFDSLNGGVTVLQPYSSSEGEKFFQGTAHAIYQNIEYIDQQDPKYLLVLSGDHIYKMDYDAMLKYHQEKKASLTVGVIHVTNEEAKRFGMMNTDATDRIIEFEEKPEHPKSDKASMGIYIFNWPTLRDYLVKSYATDKSLEDFGKNVIPSYLANNESVYAYAFKGYWRDVGTIKSLWQANMEFLSPHNRLNIGDRYWRIYSKAEVLPPMFLTETSQVNNAMVVDSCYVAGEIDHSILSQRVSVGMGSRVVDSMIMPGATIGKNVVIDHALIGEDAVIGDDAQIIGTTDKIAVVGYHETMGVEQP
|
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.
|
Q890J0
|
Q8FLJ8
|
TRPD_COREF
|
Anthranilate phosphoribosyltransferase
|
Corynebacterium
|
MTSDETLAVLIRYLDNPNPTVEEAVEVFTPMTIGEYDDVHIAALLATIRTRGETFADIAGAAKAFLNAGRPFPVPGTGVLDTAGTGGDGANTINITTGASLVAAAGGLKVVKHGNRSVSSKSGSADVLEALNIPLDLDPERAQRWFEASNFTFLFAPAYNPAIAHAQPVRKALKVPTIFNVLGPLLSPVRPEFQIMGVANPRHGQMLTEVFRELGRTRALVVHGAGTDEIAVHGTTQVWELKADGEIISYEITPEELGVERCDLTDLVGGDGVENARHMRAIFDGTGPAAHRNAVAVNAGAMFYLNSQADSLREGTAHALSLINDGTVADWLKTHEEIDYRG
|
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
|
Q8FLJ8
|
A9MFB7
|
IHFA_SALAR
|
Integration host factor subunit alpha
|
Salmonella
|
MALTKAEMSEYLFDKLGLSKRDAKELVELFFEEIRRALENGEQVKLSGFGNFDLRDKNQRPGRNPKTGEDIPITARRVVTFRPGQKLKSRVENAAPKEE
|
This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control.
|
A9MFB7
|
B1AIZ3
|
TRUB_UREP2
|
tRNA-uridine isomerase
|
Ureaplasma
|
MSAISKNIIIINKPIKWTSNDVVQKVKRVIGAKKVGHAGTLDPNASGVLVLGINEGTKLLTKLILDNKSYIAEIKFGTSTNTYDAAGEIVSSTNRMVTLTEVTKIVKDFYKNDYWQKPPQFSALKINGQKAYVLARQKVDFEIAPRLVKIFKYQIMDFNYEKQILKISLHVSKGFYVRSFAVDLATKINNLAHLLTLIRTQSGPFEIKDAIEIEQVYDYWNNINKYL
|
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
|
B1AIZ3
|
Q4Q0R9
|
MTNA_LEIMA
|
Translation initiation factor eIF-2B subunit alpha/beta/delta-like protein
|
Leishmania
|
MMSKPHHATLESIKYTPGSLRLLDQRKLPLETVFDDVLTVEDIWSAIKEMRVRGAPAIAVSAALGIAVATQRKAANGELKSGREVQTFLLTSCDFVMTSRPTAVNLFNCLRDLKAQVDKLDPTKAAAEVAQAFVELAEAVYTNDVAFNEGIMRHGAAHILAAAKAEGRDKVSILTICNTGALATSRYGTALGVVRQLFYDGKLERVYACETRPWNQGARLTVYECVQEDIPCTLICDGAASSLMLNRKIDAVVVGADRICQNGDTANKIGTYNLAVSAKFHGVKLYVAAPTTTLDVKTASGNHVEIEEREPTEITTNLVTKQRVVADGPHLSIWNPVFDITPSELITGGIITEKGVQAPAASAPYYDIASIIAQA
|
Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
|
Q4Q0R9
|
P99095
|
GLN1A_STAAN
|
Glutamine synthetase I alpha
|
Staphylococcus
|
MPKRTFTKEDIRKFAEEENVRYLRLQFTDILGTIKNVEVPVSQLEKVLDNEMMFDGSSIEGFVRIEESDMYLHPDLDTWVIFPWTAGQGKVARLICDVYKTDGTPFEGDPRANLKRVLKEMEDLGFTDFNLGPEPEFFLFKLDEKGEPTLELNDDGGYFDLAPTDLGENCRRDIVLELEDMGFDIEASHHEVAPGQHEIDFKYADAVTACDNIQTFKLVVKTIARKHNLHATFMPKPLFGVNGSGMHFNVSLFKGKENAFFDPNTEMGLTETAYQFTAGVLKNARGFTAVCNPLVNSYKRLVPGYEAPCYIAWSGKNRSPLIRVPSSRGLSTRIEVRSVDPAANPYMALAAILEAGLDGIKNKLKVPEPVNQNIYEMNREEREAVGIQDLPSTLYTALKAMRENEVIKKALGNHIYNQFINSKSIEWDYYRTQVSEWERDQYMKQY
|
Glutamine synthetase (GS) is an unusual multitasking protein that functions as an enzyme, a transcription coregulator, and a chaperone in ammonium assimilation and in the regulation of genes involved in nitrogen metabolism. It catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. Feedback-inhibited GlnA also interacts with and regulates the activity of the transcriptional regulator TnrA. During nitrogen limitation, TnrA is in its DNA-binding active state and turns on the transcription of genes required for nitrogen assimilation. Under conditions of nitrogen excess, feedback-inhibited GlnA forms a stable complex with TnrA, which inhibits its DNA-binding activity. In contrast, feedback-inhibited GlnA acts as a chaperone to stabilize the DNA-binding activity of GlnR, which represses the transcription of nitrogen assimilation genes.
|
P99095
|
Q73ZP9
|
MBTK_MYCPA
|
Mycobactin synthase protein K
|
Mycobacterium avium complex (MAC)
|
MSDAPAESAPAQIDPAQTDPAEQPVQILPRERSDIPDAVARIPRPPVPHLDPPFALRVARLGDADMVAEWMNRPHLAAAWEYDWPTPRWRRHLGAQLQGSYSLPLIGSMRGVDLAYLELYWAAKDLISRYYDAEPYDLGLHAAIADVKLVNRGLGPMLLPRIVASVFATEPRCRRVMFDPDHRNTTARRLCEYAGCRFLGEHDTTNRRMALYALDAPTTDR
|
Acyltransferase required for the direct transfer of medium- to long-chain fatty acyl moieties from a carrier protein (MbtL) on to the epsilon-amino group of lysine residue in the mycobactin core.
|
Q73ZP9
|
A7GSG2
|
RNZ_BACCN
|
tRNase Z
|
Bacillus cereus group
|
MEFVFLGTGAGVPSKGRNVSAIALQLLEERGGTWLFDCGEATQHQILHTSVRPRRIEKIFITHLHGDHIFGLPGLLGSRSFQGGTTPLTVYGPKGIEQFIEVALSVSTTHVKYPLEIVEITEEGIVFEDKQFYVETKRLSHGIECFGYRIVEKDIQGPLLVEKLREANVKPGPIFKRLKDGEIVELEDGRVLDGKDFIGPPQKGRIITILGDTRYCDASRILAQDADVLVHEATFAAADQTQAHDYFHSTTEQAARIALEANVKRLILTHISSRYQGDMYKELLREAKAVFAHTEIAMDLKSFPVER
|
Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
|
A7GSG2
|
Q68WL0
|
RHO_RICTY
|
ATP-dependent helicase Rho
|
typhus group
|
MNTTNKQLTEELNNTESNNDHNDFAENNIINLKQLKRKLPEELQVQAEELKIENISSLLKQELVFAILKKSVEQGGLIVGDGVLEVLPDGFGFLRSPEVNYLAGPDDIYISPSQIRRFGLRTGDTVEGQIRAPKAGERYFALLKVNRVNFDDPVNAYHRVHFDNLTPLYPDEKLGLELENNSKDSKDFSTRVIELVAPMGKGQRALIVAPPRTGKTVLLQNIAHAITTNNPEVFLIVLLIDERPEEVTDMQRSVRGEVVSSTFDEPASRHVQLAEMVIEKAKRLVEHKKDVVILVDAITRLARAYNTVVPSSGKVLTGGVDANALQRPKRFFGAARNIENGGSLTIIGTALIETGSRMDEVIFEEFKGTGNSEIVLDRKIADKRIYPAIDITRSGTRKEDLLVDKIILNKMWVLRRIIDPMGSSEAIEFLLKKLENTKTNYEFFEMMKSPERSRNGL
|
Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template.
|
Q68WL0
|
B1YAJ2
|
RNZ_PYRNV
|
tRNase Z
|
Pyrobaculum
|
MPLLKLVFLGTGGAVPRSDRTLPAIYLEDWLGHRFLLDAGEGAQYRLLQIGVSPASLTAVAITHQHEDHTLGLPGLVITSRFLGGRTAVLAPRSMHKALEALGVEVMDSYGGDRLRVSCVEVCHTVDACGWLFQWDVGYKLDLSKAAGLPRWALTSLIRGSPVEVGGRLIKPEDVAEPGHKRLRRLLYTGDTAPCPEMWRKVGEVDVLIHEATFADDVEPQKAHEEGHSTVADAVEAAKALNAGVLILTHVSSRYPDKRRHRELAASVKPPPHVYVPEDFDTVLVRL
|
Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
|
B1YAJ2
|
P20457
|
PRI2_YEAST
|
DNA primase 58 kDa subunit
|
Saccharomyces
|
MFRQSKRRIASRKNFSSYDDIVKSELDVGNTNAANQIILSSSSSEEEKKLYARLYESKLSFYDLPPQGEITLEQFEIWAIDRLKILLEIESCLSRNKSIKEIETIIKPQFQKLLPFNTESLEDRKKDYYSHFILRLCFCRSKELREKFVRAETFLFKIRFNMLTSTDQTKFVQSLDLPLLQFISNEEKAELSHQLYQTVSASLQFQLNLNEEHQRKQYFQQEKFIKLPFENVIELVGNRLVFLKDGYAYLPQFQQLNLLSNEFASKLNQELIKTYQYLPRLNEDDRLLPILNHLSSGYTIADFNQQKANQFSENVDDEINAQSVWSEEISSNYPLCIKNLMEGLKKNHHLRYYGRQQLSLFLKGIGLSADEALKFWSEAFTRNGNMTMEKFNKEYRYSFRHNYGLEGNRINYKPWDCHTILSKPRPGRGDYHGCPFRDWSHERLSAELRSMKLTQAQIISVLDSCQKGEYTIACTKVFEMTHNSASADLEIGEQTHIAHPNLYFERSRQLQKKQQKLEKEKLFNNGNH
|
DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication. In a complex with DNA polymerase alpha (DNA polymerase alpha:primase) constitutes a replicative polymerase. Both primase components participate in formation of the active center, but the ATP-binding site is exclusively located on p48.
|
P20457
|
Q8PML8
|
LPXB_XANAC
|
Lipid-A-disaccharide synthase
|
Xanthomonas
|
MKGIGNRESGIVDGQRNGASVGSVTTALPIPDSPLPIPGARKRAPRIALIAGEASGDILGAGLIEQLRLRYPNAEFVGIGGDAMRGVGCQTWFDASELAVMGLTEVLRHLPRLLKLRSAFRERVLAWKPDVFIGIDAPDFNLPVERWLKQRGIKTVHYVSPSVWAWREKRAEKIGVSADLVLCLFPMEPPIYAKHGVDARFVGHPMADDIAYQSDRAAARATLGLSASSTVLAVLPGSRHGEISRLGDTFFQAAWLVSEHLPNLHVLVPAANPGCKQLLAEQLSRSSLPVMRSHLLDGQARTAMLAADVVLLASGTATLEAMLVKRPMVVGYKVAPLTYRIVKLLGLLKVNRYALPNILANDDLAPELMQDDCTPERLCVALLDWFKHPDKVAALQPRYLALHAELRRDASARAADAVAGLLSQRESGMENRESAGAGA
|
Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
|
Q8PML8
|
Q3YR20
|
HSLV_EHRCJ
|
ATP-dependent protease subunit HslV
|
Ehrlichia
|
MEHKDPSQMYGTTILCIRRGNQVIIAGDGQVSLGQTVIKNSAKKIKRLANDTVITGFAGATADAFTLFERLESKLEKHPGQLLRACVELAKDWRMDKYLRRLEAMMIVADKSISLIISGNGDVLEPENGIAAIGSGGNYALAAAKALCETNERFSQNMTLEYTITTAMRIASEICIYTNNNIIIEKIED
|
Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
|
Q3YR20
|
B5ZYU8
|
RS14_RHILW
|
30S ribosomal protein S14
|
Rhizobium
|
MAKTSAVEKNKRRRTTVANQAAKRAALKAIIMNQALPIEERFKASIKLASLPRDGSKTRIRNRCEVSGRPRAYYRKLRMSRIALRELGNLGKVPGIVKSSW
|
Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site.
|
B5ZYU8
|
Q6GM84
|
GFRP_XENLA
|
GTP cyclohydrolase I feedback regulatory protein
|
Xenopus
|
MPYVLISTQIRMETGPTIVGDEFSDLVLMAQLEADKRTVLGNNFSEYYVNEPPRVTLNKLERLGYRVVSMTGVGQTLVWCLHKE
|
Mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase 1.
|
Q6GM84
|
Q9VRJ0
|
GEN_DROME
|
Xpg-like endonuclease
|
Sophophora
|
MGVKELWGVLTPHCERKPINELRGKKVAIDLAGWVCESLNVVDYFVHPRHHLKNLFFRTCYLIWEQVTPVFVLEGVAPKLKSQVIAKRNELQFRGVKPKNSPECTQSQPSKGDKGRSRFNHVLKQCETLLLSMGIQCVQGPGEAEAYCAFLNKHGLVDGVISQDSDCFAYGAVRVYRNFSVSTQGAQAAAGGAVDIYDMREITSRMDFGQQKIIVMALLCGCDYCPDGIGGIGKDGVLKLFNKYKETEILDRMRSWRGETDKYNALEIRVDDKSICSNCGHIGKTQSHTKSGCSVCRTHKGCDESLWKEQRLSIKSELTLRRKALLSPDFPNEEIIAEFLSEPDTIPNLNLNWRQPNLVKFIKQIGHLLQWPEIYCFQKFFPILTRWQVQQSKQEKILIQPHEIIKKRTVKGVPSLELRWHDPSGIFKGLIPDKQIAEYEAEHPKGIEELYYTIEPLDMLETAYPDLVAAFLKSKEKPAKKTTRKKKTASEEENKENEPNSKPKRVVRKIKAQPEENQPLLHQFLGRKKEGTPVKAPAPQRQQCSTPITKFLPSDLESDCDAEEFDMSDIVKGIISNPNAKPALTNHDGHQLHYEPMAEDLSLRLAQMSLGNVNESPKVETKRDLSQVDQLPQSKRFSLEDSFDLLVKGDLQKLARTPVERFKMQHRISEKIPTPVKPLDNISYFFNQSSDNADVFEELMNSSLVPQDQEDNAEDEEEDDLVVISD
|
Endonuclease which cleaves flap structures at the junction between single-stranded DNA and double-stranded DNA. Specific for 5'-overhanging flap structures in which the 5'-upstream of the flap is completely double-stranded. Prefers the blocked-flap structures similar to those occurring at replication forks, in which the 5' single-strand overhang of the flap is double-stranded. Also possesses weak 5'- to 3'-exonuclease activity on nicked but not gapped double-stranded DNA. Does not cleave bubble-like or Holliday junction substrates.
|
Q9VRJ0
|
D1Z6B1
|
UTP25_SORMK
|
U three protein 25
|
Sordaria
|
MAFRGRGGDRGGGGRGRGGGGGFRGRGGSRGGGSRGGDRGGSRGRGRGGDRGASRGRGRGSSRGGARGGFGPRPSKFNDARLADKDEDGSEEDDISEDESNVSEEEIEGSEEEDEEGEEEAQSGQPYMSLLKSFQSATKSKKRKLDHTEEEGPNKATKTEDDDDSDDEDDDEEVKEDVDAVDEPEEDPQDAPLEDLFDEDDDLDDSDPFETHFAAPDEATFQARIKAVQANKWRTDRIAQNSNRIYYNTPETGDSTERKLPHSISGVADLKLKKKLAESMAKHTEFDEAEKAVAPLLFNYQDMLYCNRTVASSESIRRMACLHALNHVFKTRDRVIKNNTKLQRDDTLELRDQGFTRPKVLMLLPTRQSCVKMVEMICEVASPEQQEHRKRFDEGYVDKSTKFSDDKPEDFRDLFSGSDDDMFRLGMKFTRKTIKYFSQFYNSDIIFASPLGLRMAIGSEEEKKKLDYDFLSSIELVIVDQADALLMQNWEHVEFIFEHLNLQPRDAHGCDFSRVRPWYLDDQAKYFRQTVIFSAFNTPELAELQRLHCHNWAGKARLHPEYPGVIQYLGVKTRQTFSRFDAGSIAADPDARFAYFTKAIVPTLVKRAKDAAGTLIFIPSYLDFVRVRNYFANNPDVASVTFGNISEYADTPEASRARSHFLTGRHRVLLYTERAHHFRRYAIKGVKRVIFTKSEQSLMLEHGLGTVKVMFSKYDIMKLERIVGTKRAGKMITEQGDTFDFV
|
DEAD-box RNA helicase-like protein required for pre-18S rRNA processing, specifically at sites A0, A1, and A2.
|
D1Z6B1
|
Q8VQX6
|
RECX_MYXXD
|
Regulatory protein RecX
|
Myxococcus
|
MDEARGGPDKKKERGPKRPRKVSPTYLENAALHYLKRYAATKSQLQRVLLRRVDRSIKFHGGERGEALAWVEALVAKLVRNGLLNDEAYAQMKAHSLRASGRSTRVIAQKLRLKGVPAEVVAKKVADATHEVSEEDAARIWARKKRLGPFRTQPGTREENRKRDLAALARAGFSFGIAKKVIDSNPA
|
Modulates RecA activity.
|
Q8VQX6
|
Q92622
|
RUBIC_HUMAN
|
Beclin-1 associated RUN domain containing protein
|
Homo
|
MRPEGAGMELGGGEERLPEESRREHWQLLGNLKTTVEGLVSTNSPNVWSKYGGLERLCRDMQSILYHGLIRDQACRRQTDYWQFVKDIRWLSPHSALHVEKFISVHENDQSSADGASERAVAELWLQHSLQYHCLSAQLRPLLGDRQYIRKFYTDAAFLLSDAHVTAMLQCLEAVEQNNPRLLAQIDASMFARKHESPLLVTKSQSLTALPSSTYTPPNSYAQHSYFGSFSSLHQSVPNNGSERRSTSFPLSGPPRKPQESRGHVSPAEDQTIQAPPVSVSALARDSPLTPNEMSSSTLTSPIEASWVSSQNDSPGDASEGPEYLAIGNLDPRGRTASCQSHSSNAESSSSNLFSSSSSQKPDSAASSLGDQEGGGESQLSSVLRRSSFSEGQTLTVTSGAKKSHIRSHSDTSIASRGAPESCNDKAKLRGPLPYSGQSSEVSTPSSLYMEYEGGRYLCSGEGMFRRPSEGQSLISYLSEQDFGSCADLEKENAHFSISESLIAAIELMKCNMMSQCLEEEEVEEEDSDREIQELKQKIRLRRQQIRTKNLLPMYQEAEHGSFRVTSSSSQFSSRDSAQLSDSGSADEVDEFEIQDADIRRNTASSSKSFVSSQSFSHCFLHSTSAEAVAMGLLKQFEGMQLPAASELEWLVPEHDAPQKLLPIPDSLPISPDDGQHADIYKLRIRVRGNLEWAPPRPQIIFNVHPAPTRKIAVAKQNYRCAGCGIRTDPDYIKRLRYCEYLGKYFCQCCHENAQMAIPSRVLRKWDFSKYYVSNFSKDLLIKIWNDPLFNVQDINSALYRKVKLLNQVRLLRVQLCHMKNMFKTCRLAKELLDSFDTVPGHLTEDLHLYSLNDLTATRKGELGPRLAELTRAGATHVERCMLCQAKGFICEFCQNEDDIIFPFELHKCRTCEECKACYHKACFKSGSCPRCERLQARREALARQSLESYLSDYEEEPAEALALEAAVLEAT
|
Involved in regulation of pathogen-specific host defense of activated macrophages. Following bacterial infection promotes NADH oxidase activity by association with CYBA thereby affecting TLR2 signaling and probably other TLR-NOX pathways. Stabilizes the CYBA:CYBB NADPH oxidase heterodimer, increases its association with TLR2 and its phagosome trafficking to induce antimicrobial burst of ROS and production of inflammatory cytokines . Following fungal or viral infection (implicating CLEC7A (dectin-1)-mediated myeloid cell activation or DDX58/RIG-I-dependent sensing of RNA viruses) negatively regulates pro-inflammatory cytokine production by association with CARD9 and sequestering it from signaling complexes .
|
Q92622
|
Q11184
|
LE756_CAEEL
|
Lethal protein 756
|
Caenorhabditis
|
MAVPAASSIVSYGGAATSNFLTTPVTPFLAGFYNSNFVTDRINSCAPYRVDRIRKQLQDEEENGYPPADDRRRGALFCRSGTWLEMLPIENPDDGSTRVKVHGTKEESSKFSIVEFVSVAMSLVSIRGVETKNFICMDPSGKLYATPSSNYSTECVFLEEMMENYYNLYASCAYGDRFNPWYIELRRSGKPRRGPNSKKRRKASHFLVVHHDLDRLRSPVPNGNDVTDLVVASLFHQPPSHPLFRQQTVTKPPNPHRISNLRAKVEMTNQAEKQRLLEEKKRRREKKKRRREDRLRKEEQIREARRQELKSLREEELRRRYQQQQQQQASTQTRYNRPQNPANPYPTYRPLPTRSTVQSPRPAYNPYWQSPVTQAPHHNSHHHHHHHPRVSSSSDPQQRHQSQQHYLAQTVSNPNRQNVNYQRYP
|
Required for larval development . Probably by binding receptor egl-15, regulates negatively membrane protrusion from body wall muscles during larval development .
|
Q11184
|
Q8EK53
|
RL18_SHEON
|
50S ribosomal protein L18
|
Shewanella
|
MDKKTSRLRRAIRARKKIQELGVNRLVVHRTPRHIYAQVINPEAQVVAAASTVEKAVKEQLKSTGNVDAAKAVGKFVAERAIEKGVTNVAFDRSGFKYHGRVAALADAAREAGLQF
|
This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
|
Q8EK53
|
Q56226
|
NQO11_THET8
|
NDH-1 subunit 11
|
Thermus
|
MSYLLTSALLFALGVYGVLTRRTAILVFLSIELMLNAANLSLVGFARAYGLDGQVAALMVIAVAAAEVAVGLGLIVAIFRHRESTAVDDLSELRG
|
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient required for the synthesis of ATP.
|
Q56226
|
Q6D157
|
PLSY_PECAS
|
Lysophosphatidic acid synthase
|
Pectobacterium
|
MSVTALGMMLIAYLCGSVSSAILFCKITGLPDPRLHGSGNPGATNVLRIGGKAAAATVLVFDILKGMLPVWGAYALGVTPLYLGLTAIAACLGHIYPVFFHFRGGKGVATALGAIAPIGLDLTGLMTGTWLLTVLLSGYSSLGAIVSALIAPFYVWWFKPQFTFPVAMLSCLILMRHHDNIQRLWRGQESKIWDKLRKKKQPEDEDTSPEE
|
Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
|
Q6D157
|
C5GDJ2
|
RCF1_AJEDR
|
Respiratory supercomplex factor 1, mitochondrial
|
Blastomyces
|
MPNIDNTPLPSSFDAHPEFFQETKWQKVTRRLKEEPLIPIGYAATSYALWRAYKSMKARDSVELNRMFRARIYGHAFTLFAIVAGGIYYGQERKQRKEFEKALQEKQDQEKRDAWLRELEVRDKEDKDWRQRHAAMEMAAKEAEKKMG
|
Cytochrome c oxidase subunit which plays a role in assembly of respiratory supercomplexes.
|
C5GDJ2
|
Q57K67
|
YGFZ_SALCH
|
tRNA-modifying protein YgfZ
|
Salmonella
|
MAFISFPPRHPSSSARLPLTLIALDDWALSTITGVDSEKYIQGQVTADVSQMTEQQHLLAAHCDAKGKMWSTLRLFRERDGFAWIERRSVLEAQLTELKKYAVFSKVVIAPDDERVLLGVAGFQARAALANVFSVLPNSENQVVRDGASTLLWFEHPAERFLLVTDVATANMLTEKLHGEAELNNSQQWLALDIEAGIPAIDAANSGQFIPQATNLQALGGISFKKGCYTGQEMVARAKFRGANKRALWLLAGKASRVPEAGEDLELQMGENWRRTGAILAATQLDDGQLLVQAVMNNDLEAESVFRVRDDANTLHIVPLPYSLEE
|
Folate-binding protein involved in regulating the level of ATP-DnaA and in the modification of some tRNAs. It is probably a key factor in regulatory networks that act via tRNA modification, such as initiation of chromosomal replication.
|
Q57K67
|
Q1C5W7
|
MACB2_YERPA
|
Macrolide export ATP-binding/permease protein MacB 2
|
Yersinia
|
MTGPQQGKILLRLENVSREFITGEQTVRVLNNINLTLHSGEMVAIVGTSGSGKSTLMNILGCLDKPSAGEYWVAGRIPQYLGSDALAELRREHFGFIFQRYHLLNDLSARENVEIPAIYAGIDREERRKRAVNLLSRIGLAERLDYRPSQLSGGQQQRVSIARALMNGGDVILADEPTGALDTHSGNEVLNILKDLHQQGHTVVIVTHDMSIAEHAQRIIELKDGEIIADRPRDHAQEKPKMVDIPSVIDIPSMDEKISTGAQQETEIARKPLLTRWKVQYDRLHEAFKMAILAMAAQRLRTALTMLGIIIGIASVVSVVALGKGSQQQVLANINAMGTSTLEIFPGKDFGDMRSAAIHTLRDTDADVLAQQGYIHSVTPTVSTSVTLRYGNKSVSGTVNGVGEQYFLVRGYTIAQGMAFTRTSVNDLMQDAVIDENTRDKLFPNGETPLGKVILLGSLPCRVIGVAAKKQSGFGSDENLNVWIPYTTAMKRMLGQSYLKSITVRVNDDIDLANAEQGVIKLLSQRHGTQDFFVMNTDSIRQTIQATTSTMTLLVSMIAVISLIVGGIGVMNIMLVSVTERTKEIGVRMAVGARASDIMQQFLIEAVLVCLLGGSLGVALSLGIGLLFSLFSSNFSMVYSAASIITAFVCSSLIGVIFGFFPAKRAAEMDPIRALERE
|
Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.
|
Q1C5W7
|
Q9SFW8
|
NLP5_ARATH
|
Nodule inception protein-like protein 5
|
Arabidopsis
|
MENNSLPMDPAMDSSFMDGLLLEGCWLETTDASEFLNFSPSTSVAPFDPSSFMWSPTQDTSNSLSQMYGQDCPERSSLEDQNQGRDLSTFNRRWWIGPSGHHGFSVMERLVQAVTHIKDFTSERGSLIQLWVPVDRGGKRVLTTKEQPFSHDPMCQRLAHYREISENYQFSTEQEDSDSSSRDLVGLPGRVFLGKVPEWTPDVRFFKNEEYPRVQHAQDCDVRGTLAIPVFEQGSQICLGVIEVVMTTQMVKLSPDLESICRALQAVDLRSTEIPIPPSLKGPDFSYQAALPEIRNLLRCACETHKLPLAQTWVSCLKQSKTGCRHNDENYIHCVSTIDDACYVGDPTVREFHEACSEHHLLKGQGVVGEAFLTNGPCFSSDVSSYKKSEYPLSHHATMFGLHGTVAIRLRCIHTGSVDFVLEFFLPKNCRDIEEQRKMLNALSTIMAHVPRSLRTVTQKELEEEGDSMVSEVIEKGVTLPKIENTTEVHQSISTPQNVGLVFDGGTTEMGELGSEYGKGVSVNENNTFSSASGFNRVTEKKRTKAEKNITLDVLRQYFAGSLKDAAKSIGVCPTTLKRICRQHGIQRWPSRKIKKVGHSLQKIQRVIDSVEGVSGHHLPIGSFYASFPNLAASPEASSLQQQSKITTFLSYSHSPPAKSPGSSCSHSSSCSSETQVIKEDPTDKTRLVSRSFKETQTTHLSPSSQEDDFLRVKVSYEEEKIRFKMRNSHRLKDLLWEIAKRFSIEDVSRYDLKYLDEDNEWVLLRCDDDVEECVDVCRSFPGQTIKLLLQLSSSYLPERSSVSGCLS
|
Probable transcription factor.
|
Q9SFW8
|
B8E4U3
|
RPIA_SHEB2
|
Phosphoriboisomerase A
|
Shewanella
|
MTQDEMKKAAGWAALKYVERDSIVGVGTGSTVNHFIDALATMKADIEGAVSSSEASTQKMKALGIPVYDLNSVDRLSVYVDGADEINDRMDMIKGGGAALTREKIVAAVAEKFICIVDNTKQVDILGEFPLPVEVIPMARSYVARQLVKLGGDPVYREGVVTDNGNVILDVYNLKILNPKELESQINEIVGVVTNGLFAKRGADVLLVGTPDGVKTFTAE
|
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
|
B8E4U3
|
Q48KN0
|
AROC_PSE14
|
5-enolpyruvylshikimate-3-phosphate phospholyase
|
Pseudomonas
|
MSGNTFGKLFTVTTAGESHGPALVAIVDGCPPGLELDLQDLQRDLDRRKPGTSRHTTQRQEADEVEILSGVFEGKTTGASIGLLIRNTDQKSKDYSAIKDLFRPAHADYTYHHKYGIRDYRGGGRSSARETAMRVAAGAIAKKYLATQGIVIRGYMSQLGPIQIPFKTWDSVEDNAFFCPDPDKVPELEAYMDQLRRDQDSVGAKITVVAEGVMPGLGEPIFDRLDAELAHALMNINAVKGVEIGAGFDCVAQRGTEHRDEMTPLGFLSNQAGGILGGISSGQPIIAHLALKPTSSITTPGRSIDTDGNAADVITKGRHDPCVGIRATPIAEAMMAIVLLDHLLRHRGQNADVSVNTPVLGQL
|
Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
|
Q48KN0
|
Q68VW6
|
SYS_RICTY
|
Seryl-tRNA(Ser/Sec) synthetase
|
typhus group
|
MLNIKWIRENQELFDEKLSQRFIEPMSSKIAMLDREKRKITSLIQEFQHARKVKSKILGNMVSKSGEEFEELQRDVNHINEKLEELEQTLDNNNELNELLNMLPNIPDEEVPYGIDESMNKLVRSYGNTNKNALNKQHFELGTKLNLMDFEQTAKISGSRFVTLKGDLAKLERALINFMVDIHTKEFDFFEISPPLLVRDSAMYNAGQLPKFSEESFITTNGYRLIPTAEVSLVNIVADTIIQREKLPMRYVAYTTCFRSEAGSSGRDTRGMIRLHQFGKVELVSITTPEESKNEHEYITNASETILKKLDLPYRVMLLCTGDMGFAAKKTYDIEVWLPGQNQYREIASCSNCGDFQARRMKARYKEFGSNETTLVHTLNASGLPIGRTIVAILENYQNNDGSITIPDVLINYMGGLKKITTYSE
|
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).
|
Q68VW6
|
C3K613
|
FADB_PSEFS
|
3-hydroxyacyl-CoA dehydrogenase
|
Pseudomonas
|
MIYEGKAITVKALESGIVELKFDLKGESVNKFNRLTLNELRQAVDTIKADASIKGVIVSSGKDVFIVGADITEFVDNFKLPDAELVAGNLEANKIFSDFEDLNVPTVAAINGIALGGGLEMCLAADFRVMSATAKIGLPEVKLGIYPGFGGTVRLPRLIGADNAIEWIAAGKENRAEDALKVGAVDAVVAPDKLAEAALNLIKGAISGEFDYKAKRQPKLEKLKLNAIEQMMSFETAKGFVAGQAGPNYPAPVEAIKTIQKAANFGRDKALEVEAAGFVKLAKTSAAQSLIGLFLNDQELKKKAKAYDEIARDVKQAAVLGAGIMGGGIAYQSASKGTPILMKDINEHGIEQGLAEAAKLLVGRVDKGRMTAAKMAEVLNGIRPTLSYGDFGHVDLVVEAVVENPKVKQAVLAEVEAQVKDDTILASNTSTISISLLAKALKRPENFVGMHFFNPVHMMPLVEVIRGEKSSELAVATTVAYAKKMGKNPIVVNDCPGFLVNRVLFPYFGGFAKLVSAGVDFVRIDKVMEKFGWPMGPAYLMDVVGIDTGHHGRDVMAEGFPDRMKDDRRSAIDALYEAKRLGQKNGKGFYAYEADKKGKQKKVADPSVHEVLAPVIYEQREVSDEDIINWMMIALCLETVRCLEDGIVETAAEADMGLVYGIGFPPFRGGALRYIDSIGVAEFVALADKYADLGPLYHPTAKLREMAKNGQSFFG
|
Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate.
|
C3K613
|
P20966
|
PTFBC_ECOLI
|
Fructose permease IIC component
|
Escherichia
|
MKTLLIIDANLGQARAYMAKTLLGAAARKAKLEIIDNPNDAEMAIVLGDSIPNDSALNGKNVWLGDISRAVAHPELFLSEAKGHAKPYTAPVAATAPVAASGPKRVVAVTACPTGVAHTFMAAEAIETEAKKRGWWVKVETRGSVGAGNAITPEEVAAADLVIVAADIEVDLAKFAGKPMYRTSTGLALKKTAQELDKAVAEATPYEPAGKAQTATTESKKESAGAYRHLLTGVSYMLPMVVAGGLCIALSFAFGIEAFKEPGTLAAALMQIGGGSAFALMVPVLAGYIAFSIADRPGLTPGLIGGMLAVSTGSGFIGGIIAGFLAGYIAKLISTQLKLPQSMEALKPILIIPLISSLVVGLAMIYLIGKPVAGILEGLTHWLQTMGTANAVLLGAILGGMMCTDMGGPVNKAAYAFGVGLLSTQTYGPMAAIMAAGMVPPLAMGLATMVARRKFDKAQQEGGKAALVLGLCFISEGAIPFAARDPMRVLPCCIVGGALTGAISMAIGAKLMAPHGGLFVLLIPGAITPVLGYLVAIIAGTLVAGLAYAFLKRPEVDAVAKAA
|
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II FruAB PTS system is involved in fructose transport.
|
P20966
|
C3PAJ0
|
ACCD_BACAA
|
Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
|
Bacillus cereus group
|
MLRDLFVKKKKYAAIPSEQVRKDVPDGVMTKCPKCKKIMYTKEVLKNLKVCVNCGYHHPMNAWERLDSILDEGSFREYDKEMVSLNPLEFPNYEEKLESDRKKTELNEAVVTGEGTIDDMLVVVAVMDSRFRMGSMGSVVGEKIARAVEKAYDLQVPFIIFTASGGARMQEGILSLMQMAKTSVALKKHSNAGGLFISVMTHPTTGGVSASFASLGDYNLAEPGALIGFAGRRVIEQTVREKLPEDFQTAEFLLEHGQLDAVVHRDDMRESLRKILEVHQGGEMAVWQS
|
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.
|
C3PAJ0
|
Q8JIR6
|
DMT1Y_ORYLA
|
Y-specific doublesex- and mab-3-related transcription factor
|
Oryzias
|
MSKEKQCRPGPRVPKCSRCRNHSLKTPLKGHKRFCRWKDCHCLKCKLIVDRQRVMAAQVALRRQQAQEEELGICSPEASSGPEVVVKNEAGADCLFSVEGRSGTPAPPPNPNPLSVAGSYSASSSSPSAAARVYSEEASDQPLETSYYNFYQPSRYSSYYGNLYNYQQYQQMPPSDGRLSGHSMPSQYRMHSFYPGTAYLPQGLGSPVPPYFSLEDNDGAAASFFPSSLTSTHDSTLTYRSISSLVNDGVKAEFESGGQPPSSRPTP
|
Transcription factor that plays a key role in male sex determination and differentiation by controlling testis development and germ cell proliferation. Acts both as a transcription repressor and activator.
|
Q8JIR6
|
Q2NFX1
|
RS14Z_METST
|
30S ribosomal protein S14 type Z
|
Methanosphaera
|
MARKYGKAARKCSRCGDHSAIVRRYGLNLCRQCFREIAPKIGFKKYN
|
Binds 16S rRNA, required for the assembly of 30S particles.
|
Q2NFX1
|
Q5NZS9
|
PSRP_AROAE
|
Pyruvate, water dikinase regulatory protein
|
Aromatoleum
|
MSDTPIRTVFFISDGTGITAETLGHSLLAQFPGARFRQVRVPFVDDLDKALDCARQIRETAVTDGVRPIVFSTLVNPDPLSGLREIDALFVDLFEQFINPLEAELGQRSTHTVGRFHGIAESSDYKARIEAINFAMAHDDGVSTDGELADADVILVGVSRSGKTPTSLYLAVQFGVKAANYPLIPEDFERNKLPGELHRHRSKLFGLTIAPERLSQIRQERRPNSRYASIENCRFEIDAAQKLMRRENIQWLDSTSKSIEEISATILQAVRLNRPVY
|
Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the phosphoenolpyruvate synthase (PEPS) by catalyzing its phosphorylation/dephosphorylation.
|
Q5NZS9
|
A8FRE9
|
ASTD_SHESH
|
Succinylglutamic semialdehyde dehydrogenase
|
Shewanella
|
MTQFIKGQWVAGLGHAVTSKNPANNDVIWNSQTATPEQVNTAVEAAREVQFDWFMLGFEARLAIVEAYRAQLEENKAEIAETIAQETGKPQWETATEAGAMIGKIGLSVAAYNKRTGTSENDTPAGRAVLRHKPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPKVAELMLKLWEKAGLPAGVINLVQGEVETGKALASHPQIDGLFFTGSSRTGHILHQQYAGEPGKILALEMGGNNPLIIKGVKDSKAAVHDIIQSAYISSGQRCTCARRLYVEKGAEGDALLAQLTDAVKRIVVGAWNAQPQPFMGAMISETAAKGMVEAQRNLVNLGGHSLVELTHIEEGTGLVSPGLIDVSQVIELPDEEYFGPLLQVVRYTDFDEAIKLANNTRYGLSAGILADSRDDYEYFLARIRAGIVNWNKQITGASGAAPFGGVGASGNHRASAFYAADYCAYPVASVEADEVSLPANLSPGLSL
|
Catalyzes the NAD-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
|
A8FRE9
|
Q1MPK8
|
GPMI_LAWIP
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase
|
Lawsonia
|
MNVVPILLLILDGYGLAPDSTGNAAKLAFTPNIDRMLAMSGGTQIHASGRAVGLPDGYMGNSEVGHLNIGAGRVVYQQMTRIDVAIENKELDSNPILLDLFTKVKSSNGRLHLLGLLSNGGVHSHIRHLEALLSIAKEHNIQVILHPFMDGRDTGPKDGLKFMKEIVSFLTSTSSGVIGSFCGRFYAMDRDKRWERIKLAWDAIVHGVGLHVEDSVKALEQAYASGETDEFIKPRVMGNSSVNCVQDNDAVLFFNFRADRARELVSAFILPDFNGFDRGRVPHLSGIATMTMYDKEFNIPVLFNHENITKTLGEVVSALGLLQLRIAETEKYAHVTYFFSGGREEVFTGEERILVQSPRDVATYDLKPEMSVMEVTDRLLTAWNSKKFSLIVCNLANPDMVGHTGNIKASISALEAVDNCVGRIEKAVAEQHGCFILTADHGNVEEMLDKSGQPQTAHSCNPVPLIAIYDGKPLNLKESGKLGDIAPTILSIWDVSIPNEMTGNNLLSSE
|
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
|
Q1MPK8
|
B1AJP2
|
RSMA_UREP2
|
S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase
|
Ureaplasma
|
MNKSFIKNKLKQESFVPSKKMGQNFLLSNNIKNKIVDVANINKDDLILEIGPGWGAITEILVQKTNILIAIELDKRLYAHLKTYIKTSNFHIINNDVLCVDLDNLILDYNNTQKIQKIKVVANLPYAISSKIVLKIIQSKLINDAYIMVQKEMAERIGAKVNTRGYNAFTVLVQLFCKTKILFEVNAKEFHPQPKVQSAVIHLENLHNSVNFNIEELGKFLRICFLNKRKKLKNNLSNIYDIKIINQMFIDYNLDMNLRAENIEPKMFLKLFNYLNR
|
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.
|
B1AJP2
|
Q6ZJJ1
|
APX4_ORYSJ
|
OsAPx4
|
Oryza sativa
|
MAAPVVDAEYLRQVDRARRHLRALISSKGCAPIMLRLAWHDAGTYDVNTKTGGANGSIRYEEEYTHGSNAGLKIAIDLLEPIKAKSPKITYADLYQLAGVVAVEVTGGPTVEFIPGRRDSSVCPREGRLPDAKKGALHLRDIFYRMGLSDKDIVALSGGHTLGRAHPERSGFEGAWTQEPLKFDNSYFLELLKGESEGLLKLPTDKALLEDPSFRRYVDLYARDEDTFFKDYAESHKKLSELGFTPRSSGPASTKSDLSTGAVLAQSAVGVAVAAAVVIVSYLYEASKKSK
|
Plays a key role in hydrogen peroxide removal.
|
Q6ZJJ1
|
C6DHH1
|
ILVD_PECCP
|
Dihydroxy-acid dehydratase
|
Pectobacterium
|
MPKYRSATTTHGRNMAGARALWRATGMTDNDFGKPIIAVVNSFTQFVPGHVHLRDLGKLVAEQIEASGGVAKEFNTIAVDDGIAMGHGGMLYSLPSRELIADSVEYMVNAHCADAMVCISNCDKITPGMLMASLRLNIPVIFVSGGPMEAGKTKLSDQIIKLDLVDAMIQGADPKVSDEQSEQVERSACPTCGSCSGMFTANSMNCLTEALGLSQPGNGSLLATHADRKQLFLNAGKRIVGLAKRYYEQDDESVLPRNIANKAAFENAMILDIAMGGSTNTVLHLLAAAQEGEVDFTMTDIDRLSRQVPHLCKVAPSTQKYHMEDVHRAGGVIGILGELDRAGLLNREVNNVLGKTLPETLEAYDVMLTQDDSVKSMYSAGPAGIRTTQAFSQDCRWDSLDTDRQEGCIRSREFAYSQDGGLAVLYGNLAENGCIVKTAGVDEGSLVFRGPAKVYESQDDAVDAILGGKVVAGDVVVIRYEGPKGGPGMQEMLYPTTYLKSMGLGKSCALITDGRFSGGTSGLSIGHASPEAASGGTIALVQDGDIIAIDIPNRSIALVLDDNALASRRAAEEARGDQAWTPHNRERQVSFALRAYASLATSADKGAVRDKSKLGG
|
Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
|
C6DHH1
|
Q0TLQ1
|
MURD_ECOL5
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase
|
Escherichia
|
MADYQGKNVVIIGLGLTGLSCVDFFLARGVTPRVMDTRMTPPGLDKLPEAVERHTGGLNDEWLMAADLIVASPGIALAHPSLSAAADAGIEIVGDIELFCREAQAPIVAITGSNGKSTVTTLVGEMAKAAGVNVGVGGNIGLPALMLLDDECELYVLELSSFQLETTSSLQAVAATILNVTEDHMDRYPFGLQQYRAAKLRIYENAKVCVVNADDALTMPIRGADERCVSFGVNMGDYHLNHQQGETWLRVKGEKVLNVKEMKLSGQHNYTNALAALALADAAGLPRASSLKALTTFTGLPHRFEVVLEHNGVRWVNDSKATNVGSTEAALNGLHVDGTLHLLLGGDGKSADFSPLARYLNGDNVRLYCFGRDGAQLAALRPEVAEQTETMEQAMRLLAPRVQPGDMVLLSPACASLDQFKNFEQRGNEFARLAKELG
|
Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
|
Q0TLQ1
|
C4LF13
|
TRUA_TOLAT
|
tRNA-uridine isomerase I
|
Tolumonas
|
MRIALGIEYFGADYYGWQRQREVNSVQQELETALSRVANHPVEIQCAGRTDAGVNATGQVIHFDTTANRQMSAWTLGINAQLPDDIAVRWAHVVDDNFHARFSATARRYRYIIYNEPLRPGILAKGVSHYYHPLNADQMNEAGQLLLGERDFTSFRAAQCQSNTPFRNIMSLSVHRAGSYVILDIQANAFLHHMVRNIMGSLLLVGTGEKPKEWIGEILDAKDRTVSGATAKAEGLYLVDVTYPLHYGLPKPPLGPLWFNA
|
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
|
C4LF13
|
Q06196
|
H3_ENTHI
|
Histone H3
|
Entamoeba
|
MARTKGHIERPSNKSAKAVKNVAFKAAKKMLSKDSTKKKRAHPGAVALTEIKVLQRSTELLLRKAPFQALVREIAQVSKSDLRFQSAAISALQEAAEAYLVGLFEDTNLCAIHAKRITIMPKDMQLARRIRGERT
|
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
|
Q06196
|
P38680
|
MTR_NEUCR
|
Methyltryptophan resistance protein
|
Neurospora
|
MDSQYETKKNDPNAIMPYPESNDEHVGEVRGLGGGIMDKEPEAQEGHAKFHRLGWKRLTVVLIVEAIALGSLSLPGAFATLGMVPGVILSVGMGLICIYTAHVIGQTKLKHPEIAHYADVGRVMFGRWGYEIISFMFVLQLIFIVGSHVLTGTIMWGTITDNGNGTCSLVFGIVSAIILFLLAIPPSFAEVAILGYIDFVSICAAILITMIATGIRSSHQEGGLAAVPWSCWPKEDLSLAEGFIAVSNIVFAYSFAMCQFSFMDEMHTPSDYKKSIVALGLIEIFIYTVTGGVVYAFVGPEVQSPALLSAGPLLAKVAFGIALPVIFISGSINTVVVSRYLIERIWPNNVIRYVNTPAGWMVWLGFDFGITLIAWVIAEAIPFFSDLLAICSALFISGFSFYFPALMYFKITRNDAKSQGKKYFLDALNMLCFVIGMGILGIGTYAAIQDIMDRYDHGKVSKPYSCAPLA
|
Required for the transport of neutral aliphatic and aromatic amino acids via the N system.
|
P38680
|
Q5PC10
|
COAD_SALPA
|
Pantetheine-phosphate adenylyltransferase
|
Salmonella
|
MQKRAIYPGTFDPITNGHLDIVTRATQMFDHVILAIAASPGKKPMFTLNERVALAQKATAHLGNVEVVGFSDLMANFARDRQANILIRGLRAVADFEYEMQLAHMNRHLMPQLESVFLMPSKEWSFISSSLVKEVARHQGDVTHFLPDNVHQALMDKLK
|
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
|
Q5PC10
|
P57152
|
SECE_BUCAI
|
Protein translocase subunit SecE
|
Buchnera
|
MNKHHYNRNKHKIPEKVKWISISIFFILSFFINMCFYETQLFIRIFIISCLMLCAIGTMIYTKKGKDILLYIVMSKKEMQKIIWPKYKETLYTTFIVISVTIFISFILWSIDSVIFRLIAFIISLRF
|
Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
|
P57152
|
A8AW61
|
SSRP_STRGC
|
Small protein B
|
Streptococcus
|
MAKGEGKVVAQNKKARHDYTIVDTIEAGMVLTGTEIKSVRAARINLKDGFAQIKNGEAWLSNVHIAPYEEGNIWNQEPERRRKLLLHKKQIQKLEQETKGTGMTLVPLKVYLKDGYAKLLLGLAKGKHDYDKRESIKRREQNRDIARQMKNFNTR
|
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.
|
A8AW61
|
Q2S905
|
RPOB_HAHCH
|
Transcriptase subunit beta
|
Hahella
|
MTYSYTEKKRIRKDFGKLPAVMDVPYLLSIQLDSYHDFLQQDVAIEDRQEVGLHAAFKSVFPIVSFSGNAALEYVSYRLGQPVFDVAECQLRGVTYAAPLRVKVRLIIYDKESSTKAIKDIKEQEVYMGEVPLMTENGTFVINGTERVIVSQLHRSPGVFFDHDKGKTHSSGKLLYSARIIPYRGSWLDFEFDPKDCVFVRIDRRRKLPATILLRALGYAADEMLEMFFENSLFEVEGGEYFLDLVPSRLRGDIAIFEIKDDEGNLIVEEGRRVTARHIRQMEKAGLKRLRVPSSYLLGKVTATNIADPSTGEVIVECNTEITDDAIEKIEKAGIKRIETLYTNDLDCGPFVSDTLRIDATRSQLEALVEIYRMMRPGEPPTKESAENLFNNLFFSEERYDLSAVGRMKFNRRLGREETEGLGVLSHSDIIDVLRTLIDIRNGKGVVDDIDHLGNRRVRSVGEMAENQFRVGLVRVERAVKERLSMAESEGLMPQDLINAKPVAAAVKEFFGSSQLSQFMDQNNPLSEVTHKRRVSALGPGGLTRERAGFEVRDVHPTHYGRVCPIETPEGPNIGLINSLATYARTNTYGFLESPYRKVVDGLVTDDIEYLSAIEESDYVIAQASAAVDENGRLIDELVTVRHKNEFTVMPPEKVTLMDVSPRQVVSVAASLIPFLEHDDANRALMGSNMQRQAVPTLKAEKPLVGTGMERYVAQDSGVCVVARRGGVVVSVDAARIVVRVSDDETEAGDAGVDIYNLTKYQRSNQNTCINQRSLVMEGDEVARGDVLADGPSVDLGELALGQNMRIAFMPWNGYNFEDSILVSERVVQEDRFTTIHIQELTCVARDTKLGPEEVTADIPNVGESALAKLDDSGIIYIGAEVEPGDILVGKVTPKGETQLTPEEKLLRAIFGEKASDVKDTSLRVSTGMRGTVIDVQVFTRDGVEKDQRAKEIEQTELNKFRKDLNDEYKIVEGATFERLRSALLGQSVIGGPGLKKGDTLTEVHFNAFEKEEWFKLNMADEQLNELLEKAEGQLQERRKSIEDRYEDKKRKLQSGDDLAPGVLKIVKVYVAVKRRIQPGDKMAGRHGNKGVISAIKPVEDMPYDEQGNPVDIVLNPLGVPSRMNVGQVLETHLGAAAKGLGDKINRMLAEQKQAAEIRKFLHEIYNGIGGRNEDLDSLSDSEVLVLAANLKKGVPMATPVFDGAKEKEIKEMLRLADMDDSGQVWLYDGRTGERFERQVTVGYMYMLKLNHLVDDKMHARSTGSYSLVTQQPLGGKAQFGGQRFGEMEVWALEAYGAAYTLQEMLTVKSDDVNGRTKMYKNIVDGDHRMEPGMPESFNVLVKEIRSLGIDIELEAN
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
Q2S905
|
C4Y4V1
|
GSM1_CLAL4
|
Glucose starvation modulator protein 1
|
Clavispora
|
MSIRFPEIPGTTRAPGTSLSSRGIFPTSPGVPQIPTTPNSYSALLHPHKSEAKGKHPLSFSSSMTKRLTPQEKKARRPTSRACVFCHSKHLQCSHSRPCQNCIKRNLAHECRDVVRKRAKYMSTTEVPAVSGESSSESGRATGENGSEMGNPPDPQIAYLDGVFERSSIHESLQDSPMSTPASNFNSNFLNQEYMMLGDLISKPSSPSLDVPMMYAENPSRPFISLGQSDERPKSPEFNNFDFSSLDKAQYVSPLVSHHIYQNVQDIYANKVIDFDYPSSYHSLTSFLRQRFSFTGKSLSDSEKAKKRENLLMILRLIASYRPTFISTHKALFRPFDFQFLEMSFQRCLLDYENLSRLNASPTIIWRRTGEIVSMSNDLVALLGLNISTILSKRTFILELMYDDESIVEYFRLFESVAVGNLHSTIVTRCKLIKRPSEGIETNTSMDSDYIEFCSVWTVKRDLFDLPMMVVGQFLPVLPTPDGFRTY
|
Transcription factor which regulates nonfermentable carbon utilization.
|
C4Y4V1
|
A0KFH9
|
CYAY_AERHH
|
Iron-sulfur cluster assembly protein CyaY
|
Aeromonas
|
MKDHEYHALTDAFFQYVEDTVDAGYPDIDCERAGGVLTLSFENKTKVIINKQEPLHQIWVATRENGFHFELQGESWIDNRFGHELKTLLSKACTTQAGEPVQFP
|
Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis.
|
A0KFH9
|
B0XQ42
|
ERB1_ASPFC
|
Eukaryotic ribosome biogenesis protein 1
|
Aspergillus subgen. Fumigati
|
MNTSKASKKRKAVTRDVEEEAGVFSGDELNTGNLDGALSDNAHDLSSDEDESDSEVELIDDFSDEEDEEEEDVLDSDEIPSDGEDSAKKKSNAAPGELGAVIDDDDDDDDDESPSEEEQLNYRIEKDANGNDRFVYDEINPDDNSDYSDVDENANTIGNIPLSFYDQYPHIGYDINGKKIMRPAKGEALDALLDSIEIPKGWTGLTDPSTGKPLELSQEELELLRKVQMNEIPEDGYNPYEPIVEWFTSQQEIMPLSAAPEPKRRFVPSKHEAKRVMKIVKAIREGRILPFKPPTEEDEEDDTIVKYDLWADEAERKDHPMHIPAPKLPPPGYEESYHPPPEYLPSRKERKTWEEADPEDRDREFLPNDFGSLRRVPGYENFVKEKFERCLDLYLAPRVRRSKLNIDPESLLPKLPSPEELKPFPTACATVFRGHKGRVRTLAVDPSGLWLASGGDDGTVRVWELLTGRQLWSVKLSEEDPVNVVRWRPGKDALILAAAAGDDIFLAVPPIVDPAMEKASLDILDAGWGYAASVPPPTPAEANKKNNPPKWMRPSSSLADSGVCAVIPLRYVAKSLSWHRRGDYFVTVCPGSSTPASVAIAIHTLSKHLTQYPFRRRIKGGGPPQAAHFHPSKPILFVANQRSIRAYDLSRQLLVKILQPGARWISSFDIHPTSSTASGGDNLIVGSYDRRLLWHDLELSQRPYKTLRYHRKAIRAVKFHPGGRYPLFADASDDGSLQIFHGSVTGDMLSNATIVPLKVLKGHKITGELGVLDVDWHPREPWCVSAGADGTCRLWM
|
Component of the NOP7 complex, which is required for maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S ribosome.
|
B0XQ42
|
O67077
|
FTSH_AQUAE
|
ATP-dependent zinc metalloprotease FtsH
|
Aquifex
|
MNALKNFFIWAIIIGAAIVAFNLFEGKREFTTKVSLNEVVKLVEEGKVSYAEVRGNTAIIQTKDGQKLEVTLPPNTNLVDKMVEKGVRVEVANPEPPGGWLVNVFLSWLPILFFIGIWIFLLRQMSGGGNVNRAFNFGKSRAKVYIEEKPKVTFKDVAGIEEVKEEVKEIIEYLKDPVKFQKLGGRPPKGVLLYGEPGVGKTLLAKAIAGEAHVPFISVSGSDFVEMFVGVGAARVRDLFETAKKHAPCIIFIDEIDAVGRARGAIPVGGGHDEREQTLNQLLVEMDGFDTSDGIIVIAATNRPDILDPALLRPGRFDRQIFIPKPDVRGRYEILKVHARNKKLAKDVDLEFVARATPGFTGADLENLLNEAALLAARKGKEEITMEEIEEALDRITMGLERKGMTISPKEKEKIAIHEAGHALMGLVSDDDDKVHKISIIPRGMALGVTQQLPIEDKHIYDKKDLYNKILVLLGGRAAEEVFFGKDGITTGAENDLQRATDLAYRMVSMWGMSDKVGPIAIRRVANPFLGGMTTAVDTSPDLLREIDEEVKRIITEQYEKAKAIVEEYKEPLKAVVKKLLEKETITCEEFVEVFKLYGIELKDKCKKEELFDKDRKSEENKELKSEEVKEEVV
|
Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
|
O67077
|
Q2IHZ3
|
ACPS_ANADE
|
4'-phosphopantetheinyl transferase AcpS
|
Anaeromyxobacter
|
MILGLGLDVVEVARIQRILAGPPARAERFLARVFAPAERAYCDARQDRATRYAARFAAKEAAVKALGTPEGVRWLDLVVERGTGAPSLALDGVAADAARRMGVARVHLTLTHDGGVAVAAVILEGAGP
|
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
|
Q2IHZ3
|
Q8RHK3
|
SYV_FUSNN
|
Valyl-tRNA synthetase
|
Fusobacterium
|
MNELDKNYSPNEIEEKWYKIWEDSKYFAASLSSEKENYSIVIPPPNVTGILHMGHVLNNSIQDTLIRYNRMTGKNTLWMPGCDHAGIATQNKVERKLAEDGLKKEDIGREKFLEMTWDWKEKYGGIITKQLRKLGASLDWDRERFTMDEGLSYAVRKIFNDLYHDGLIYQGEYMVNWCPSCGTALADDEVDHEEKDGHLWQIKYPVKDSDEYIIIATSRPETMLADVAVAVHPEDERYKHLIGKTLILPLVNREIPVIADEYVDKEFGTGALKITPAHDPNDYNLGKKYNLPIINMLTPDGKIVEDYPKYAGLDRFEARKKIVEDLKAQDLFIKTEHLHHAVGQCYRCQTVIEPRVSPQWFVKMKPLAEKALEVVRNGEVKILPKRMEKIYYNWLENIRDWCISRQIWWGHRIPAWYGPDRHVFVAMDEAEAKEQAKKHYGHDVELSQEEDVLDTWFSSALWPFSTMGWPEKTKELDLFYPTNTLVTGADIIFFWVARMIMFGMYELKKIPFKNVFFHGIVRDEIGRKMSKSLGNSPDPLDLIKEYGVDAIRFSMIYNTSQGQDVHFSTDLLGMGRNFANKIWNATRFVIMNLKGFDVKSVDKTKLDYELVDKWIISRLNETAKDVKDCLEKFELDNAAKAVYEFLRGDFCDWYVEIAKIRLYNDDEDKKISKLTAQYMLWTILEQGLRLLHPFMPFITEEIWQKIKVDGDTIMLQQYPVADDSLIDVKIEKSFEYIKEVVSSLRNIRAEKGISPAKPAKVVVSTSNSEELETLEKNELFIKKLANLEELTCGTDLEAPSQSSLRVAGNSSVYMILTGLLNNEAEIKKINEQLAKLEKELEPVNRKLSDEKFTSKAPQHIIDRELRIQKEYQDKIKKLKESLKSFEE
|
Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
|
Q8RHK3
|
P47421
|
RS13_MYCGE
|
30S ribosomal protein S13
|
Mycoplasma
|
MARILGIDIPNQKRIEIALTYIFGIGLSSAKTILKKAKINPDKRVKDLSEEELVAIRNAASGYKIEGDLRREIALNIKHLTEIGSWKGIRHRKNLPVRGQRTRTNARTRKGPRKTVANKKIESK
|
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites.
|
P47421
|
A4SV64
|
COQ7_POLAQ
|
2-nonaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase
|
Polynucleobacter
|
MSLIDRFIAEFDTALRSVVGGAHSRRPTPGSGEISHANLDVAQRKHAAGLMRVNHVGEVCAQALYQSQKMLARNPQIQVMLEHSGQEEMDHLAWCETRLQELGSHPSYLNPFWYAGSFAIGMLAGLAGDRWSLGFVAETEKQVENHLESHLETLPQEDLRSRAIVDQMRIDEIEHGQAALHAGGVVLPDPVQKVMQAMSKVMTTAAYRI
|
Catalyzes the hydroxylation of 2-nonaprenyl-3-methyl-6-methoxy-1,4-benzoquinol during ubiquinone biosynthesis.
|
A4SV64
|
P60527
|
HAD_AGRTR
|
L-DEX
|
Agrobacterium tumefaciens complex
|
MKHIKAIAFDLYGTLFDVHSVIDQCEKRFPGRGREVSTLWRQKQLEYTWLRSLMNRYVTFEQATEDALRYTCRHLGFALDDAACTVLCDAYLRLQAFPEVPPRLRELRNRGLQLAVLSNGSPHSIGAVVGNAGIRDEFDHLISVDPVRVYKPHDRAYGLAEEAFGLARTSILFVSSNGWDATGARYFGFPTCWINRGGNVFEEMGQTPDWDLLGIDEIVRLFDSAEGSAPSV
|
Catalyzes the hydrolytic dehalogenation of small (S)-2-haloalkanoic acids to yield the corresponding (R)-2-hydroxyalkanoic acids . Acts on acids of short chain lengths, C(2) to C(4), with inversion of configuration at C-2 . Active with 2-halogenated carboxylic acids and converts only the S-isomer (or L-isomer) of 2-chloropropionic acid with inversion of configuration to produce R-lactate (or D-isomer) .
|
P60527
|
Q89FW1
|
PRMA_BRADU
|
Ribosomal protein L11 methyltransferase
|
Bradyrhizobium
|
MQPSPTHRASFSIGSEAAARRVVDVLTEVFFEGDAAVAAFERPDGQWDVTLHFADAPDQAWLRELVVNSAGNEIADTLAFDTVEAKDWVKASLEDLVPVPAGRFVVHGSHDRDRVAPNKLKIEIEAALAFGTGHHGTTRGCLLLLDHVLKSSRPSNVLDLGTGTGVLAIAAAKALHRAVLASDIDPPSVRVAAENGRLNEVGHHVRVIRATGFAAPDFARAGPFDLVLANILANPLRHLASPMARHLAPGARVILSGLLTHQAPAVIAAYRARGLVPLRHLRIEGWSSLLLRKVG
|
Methylates ribosomal protein L11.
|
Q89FW1
|
Q7D7P7
|
SECBL_MYCTO
|
SecB-like chaperone MT2006
|
Mycobacterium tuberculosis complex
|
MTDRTDADDLDLQRVGARLAARAQIRDIRLLRTQAAVHRAPKPAQGLTYDLEFEPAVDADPATISAFVVRISCHLRIQNQAADNDVKEGDTKDETQDVATADFEFAALFDYHLQEGEDDPTEEELTAYAATTGRFALYPYIREYVYDLTGRLALPPLTLEILSRPMPVSPGAQWPATRGTP
|
Chaperone component of an atypical, type II toxin-antitoxin chaperone (TAC) module, probably required for antitoxin HigA1 to neutralize its cognate toxin HigB1.
|
Q7D7P7
|
Q70Y13
|
PSBI_AMBTC
|
PSII 4.8 kDa protein
|
Amborella
|
MLTLKLFVYTVVIFFVSLFIFGFLSNDPGRNPGRDE
|
One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
|
Q70Y13
|
Q9JZ24
|
TRMB_NEIMB
|
tRNA(m7G46)-methyltransferase
|
Neisseria
|
MTDTAENQTQNNWQAGHPRSIRSFVLRQSHMTAAQQRAIDTLWDSFGIDYQATPADLDARFGSSRPKILEIGFGMGTATAEIARRLPETDFLAIDVHGPGVGNLLKLIDENHLENIRVMRHDAVEVVENMLQDGSLDGIHIFFPDPWHKKRHHKRRLIQAPFIAKLLPKLKTGGYIHLATDWEEYAQQMLEVLSSFDSLQNTAADYAPTPDYRPETKFEARGKRLGHGVWDLVFKRIG
|
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
|
Q9JZ24
|
Q9LTT3
|
HMG10_ARATH
|
Nucleosome/chromatin assembly factor group D 10
|
Arabidopsis
|
MSTDISPPYSQTHVEPVNGYPSDNKRCDDSSVPAKYDDLVRNSALFWEKLRAFLGLTSKTLKVPTVGGNTLDLHRLFIEVTSRGGIERVVKDRKWKEVIGAFSFPTTITSASFVLRKYYLKFLFQLEHVYYLEKPVSSLQSTDEALKSLANESPNPEEGIDEPQVGYEVQGFIDGKFDSGYLVTMKLGSQELKGVLYHIPQTPSQSQQTMETPSAIVQSSQRRHRKKSKLAVVDTQKPKCHRSGYNFFFAEQYARLKPEYHGQERSITKKIGHMWSNLTESEKQVYQDKGVKDVERYRIEMLEYKSSHESGATASTVAQ
|
Binds preferentially DNA with A/T-rich content.
|
Q9LTT3
|
A9MHG9
|
FABR_SALAR
|
HTH-type transcriptional repressor FabR
|
Salmonella
|
MGVRAQQKEKTRRSLVEAAFSQLSAERSFASLSLREVAREAGIAPTSFYRHFRDVDELGLTMVDESGLMLRQLMRQARQRIAKGGSVIRTSVSTFMEFIGNNPNAFRLLLRERSGTSAAFRAAVAREIQHFIAELADYLELENHMPRAFTEAQAEAMVTIVFSAGAEALDVGAEQRRQLEERLVLQLRMIAKGAYYWYRREQEKIAHHSE
|
Represses the transcription of fabB, involved in unsaturated fatty acid (UFA) biosynthesis. By controlling UFA production, FabR directly influences the physical properties of the membrane bilayer.
|
A9MHG9
|
B9E1C8
|
DER_CLOK1
|
GTP-binding protein EngA
|
Clostridium
|
MGKPIVAIVGRPNVGKSTLFNKLAGKRISIVEDTPGVTRDRVYAQAEWLNYNFTIIDTGGIEPENNDVIISKMRRQAQVAIETANVIIFIVDGREGLTAADKEVAQMLRKSKKPIVLVVNKIDNMKQENYIYEFYNLGIGEPISISASQGLGLGDMLDKLVENFKNEGNEDEDSEYIKIAFIGKPNVGKSSLINKLLGEERVIVSDIPGTTRDAIDSYLETDEGKFLLIDTAGVRRKSKVKEEIEKYSVIRTYTAVERADVCILMLDATHDISEQDEKIIGYAHELNKAIMVVINKWDLVDKDTKTVNKYKTSIGSSLSFMSYAPYLFISAKTGQRVNRIFKMVRECYDNYCKQIKTGILNDIIGKIVMMKEPPVVGNKRLKIYYVTQIGTKPPTFVFFVNDSKCIHFSYRRYIENQLRDSFDFTGTGIKLEFRERKE
|
GTPase that plays an essential role in the late steps of ribosome biogenesis.
|
B9E1C8
|
P01086
|
IAAE_HORVU
|
Chloroform/methanol-soluble protein CMe
|
Hordeum
|
MAFKYQLLLSAAVMLAILVATATSFGDSCAPGDALPHNPLRACRTYVVSQICHQGPRLLTSDMKRRCCDELSAIPAYCRCEALRIIMQGVVTWQGAFEGAYFKDSPNCPRERQTSYAANLVTPQECNLGTIHGSAYCPELQPGYGVVL
|
Inhibits trypsin in vitro. Probably plays a protective role through inhibition of insect midgut proteases.
|
P01086
|
P0AD67
|
MRDA_ECO57
|
Penicillin-binding protein 2
|
Escherichia
|
MKLQNSFRDYTAESALFVRRALVAFLGILLLTGVLIANLYNLQIVRFTDYQTRSNENRIKLVPIAPSRGIIYDRNGIPLALNRTIYQIEMMPEKVDNVQQTLDALRSVVDLTDDDIAAFRKERARSHRFTSIPVKTNLTEVQVARFAVNQYRFPGVEVKGYKRRYYPYGSALTHVIGYVSKINDKDVERLNNDGKLANYAATHDIGKLGIERYYEDVLHGQTGYEEVEVNNRGRVIRQLKEVPPQAGHDIYLTLDLKLQQYIETLLAGSRAAVVVTDPRTGGVLALVSTPSYDPNLFVDGISSKDYSALLNDPNTPLVNRATQGVYPPASTVKPYVAVSALSAGVITRNTTLFDPGWWQLPGSEKRYRDWKKWGHGRLNVTRSLEESADTFFYQVAYDMGIDRLSEWMGKFGYGHYTGIDLAEERSGNMPTREWKQKRFKKPWYQGDTIPVGIGQGYWTATPIQMSKALMILINDGIVKVPHLLMSTAEDGKQVPWVQPHEPPVGDIHSGYWELAKDGMYGVANRPNGTAHKYFASAPYKIAAKSGTAQVFGLKANETYNAHKIAERLRDHKLMTAFAPYNNPQVAVAMILENGGAGPAVGTLMRQILDHIMLGDNNTDLPAENPAVAAAEDH
|
Catalyzes cross-linking of the peptidoglycan cell wall.
|
P0AD67
|
B8HX52
|
NDHO_CYAP4
|
NAD(P)H dehydrogenase I subunit O
|
unclassified Cyanothece
|
MAVKKGDLVRLVEEKFVGSVEAQASDPRLPPYVFAGQGEVVDLMGEYAQVKFPVPTPNVWLRIDQLEAVK
|
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.
|
B8HX52
|
Q2IXP6
|
RS8_RHOP2
|
30S ribosomal protein S8
|
Rhodopseudomonas
|
MSTHDPISDLITRIRNAQMRSKSKVSTPGSRMRASVLEVLKSEGYIRGYASVEHPSGRSELEIELKYFDGEPVIREIERVSRPGRRVYASVKNLPRVNNGLGISVLSTPKGIMADHDARDANVGGEVLFTVF
|
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.
|
Q2IXP6
|
Q9I741
|
VGR1A_PSEAE
|
T6SS spike protein VgrG1a
|
Pseudomonas
|
MQLTRLVQVDCPLGPDVLLLQRMEGREELGRLFAYELHLVSENPNLPLEQLLGKPMSLSLELPGGSRRFFHGIVARCSQVAGHGQFAGYQATLRPWPWLLTRTSDCRIFQNQSVPEIIKQVFRNLGFSDFEDALTRPYREWEYCVQYRETSFDFISRLMEQEGIYYWFRHEQKRHILVLSDAYGAHRSPGGYASVPYYPPTLGHRERDHFFDWQMAREVQPGSLTLNDYDFQRPGARLEVRSNIARPHAAADYPLYDYPGEYVQSQDGEQYARNRIEAIQAQHERVRLRGVVRGIGAGHLFRLSGYPRDDQNREYLVVGAEYRVVQELYETGSGGAGSQFESELDCIDASQSFRLLPQTPVPVVRGPQTAVVVGPKGEEIWTDQYGRVKVHFHWDRHDQSNENSSCWIRVSQAWAGKNWGSMQIPRIGQEVIVSFLEGDPDRPIITGRVYNAEQTVPYELPANATQSGMKSRSSKGGTPANFNEIRMEDKKGAEQLYIHAERNQDNLVENDASLSVGHDRNKSIGHDELARIGNNRTRAVKLNDTLLVGGAKSDSVTGTYLIEAGAQIRLVCGKSVVEFNADGTINISGSAFNLYASGNGNIDTGGRLDLNSGGASEVDAKGKGVQGTIDGQVQAMFPPPAKG
|
Part of the H1 type VI secretion system (H1-T6SS) specialized secretion system, which delivers several virulence factors in both prokaryotic and eukaryotic cells during infection . Forms the spike at the tip of the elongating tube formed by haemolysin co-regulated protein 1/Hcp1 . Allows the delivery of the Tse6 toxin to target cells where it exerts its toxicity .
|
Q9I741
|
Q9Y6G9
|
DC1L1_HUMAN
|
Dynein light intermediate chain 1, cytosolic
|
Homo
|
MAAVGRVGSFGSSPPGLSSTYTGGPLGNEIASGNGGAAAGDDEDGQNLWSCILSEVSTRSRSKLPAGKNVLLLGEDGAGKTSLIRKIQGIEEYKKGRGLEYLYLNVHDEDRDDQTRCNVWILDGDLYHKGLLKFSLDAVSLKDTLVMLVVDMSKPWTALDSLQKWASVVREHVDKLKIPPEEMKQMEQKLIRDFQEYVEPGEDFPASPQRRNTASQEDKDDSVVLPLGADTLTHNLGIPVLVVCTKCDAISVLEKEHDYRDEHFDFIQSHIRKFCLQYGAALIYTSVKENKNIDLVYKYIVQKLYGFPYKIPAVVVEKDAVFIPAGWDNDKKIGILHENFQTLKAEDNFEDIITKPPVRKFVHEKEIMAEDDQVFLMKLQSLLAKQPPTAAGRPVDASPRVPGGSPRTPNRSVSSNVASVSPIPAGSKKIDPNMKAGATSEGVLANFFNSLLSKKTGSPGGPGVSGGSPAGGAGGGSSGLPPSTKKSGQKPVLDVHAELDRITRKPVTVSPTTPTSPTEGEAS
|
Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes. Probably involved in the microtubule-dependent transport of pericentrin. Is required for progress through the spindle assembly checkpoint. The phosphorylated form appears to be involved in the selective removal of MAD1L1 and MAD1L2 but not BUB1B from kinetochores.
|
Q9Y6G9
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.