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
|
|---|---|---|---|---|---|---|
Q46HR4
|
AROK_PROMT
|
Shikimate kinase
|
Prochlorococcus
|
MAVQSTPKTLKEKLGGRNIFLIGMMGSGKSQTGPVLAKMINYAFVDTDDVIEKASKQSISSIFEKDGEKVFRDVEKKVLKEISQHHSLVIATGGGLVTLPENWGILHQGIVIWLDLDLRRSIKRLESDHKRRPLLLGDNLAENFSQIYESRKPIYLESDLRIEVEDQSPYEVATMVAEHLQSILIDQEPQAERHTTEL
|
Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
|
Q46HR4
|
Q6GH70
|
RS14_STAAR
|
30S ribosomal protein S14
|
Staphylococcus
|
MAKKSKIAKERKREELVNKYYELRKELKAKGDYETLRKLPRDSSPTRLTRRCKVTGRPRGVLRKFEMSRIAFREHAHKGQIPGVKKSSW
|
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.
|
Q6GH70
|
A3M1X9
|
IXTPA_ACIBT
|
Nucleoside-triphosphate pyrophosphatase
|
Acinetobacter calcoaceticus/baumannii complex
|
MSTPHWFDQGSLVLASNNKGKVAEFEKLFEQLKLPVEIIPQGRLNIPDAIEDGLSFIENAIIKARHASKISGKPAMADDSGICVPVLGGAPGIYSARYAGEHGDDAANNAKLLNDLLPFRKNGEVIEGMFVCVLALVTHAEDPLPQIFQGIWHGEILEAPRGENGFGYDPLFWLPELQVSSAELSKEEKNKISHRGQAMQLFRESLV
|
Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
|
A3M1X9
|
Q2FT22
|
TFE_METHJ
|
Transcription initiation factor TFIIE
|
Methanospirillum
|
MASHEEILADKAIFAYLHRMIGDEGIELIRRFPTDKEYSDEELAEVTKINLNSVRNTLYTLYEHRLAKYRRIKNNETGWLTYLWELELDNMYDSVSKDLEIILEKLRKRYKYESENAFYNCPNCGNTITFSDAMDSQFVCQECENKMVHFDNDLLVNALQKRIARIEENLGHV
|
Transcription factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Facilitates transcription initiation by enhancing TATA-box recognition by TATA-box-binding protein (Tbp), and transcription factor B (Tfb) and RNA polymerase recruitment. Not absolutely required for transcription in vitro, but particularly important in cases where Tbp or Tfb function is not optimal. It dynamically alters the nucleic acid-binding properties of RNA polymerases by stabilizing the initiation complex and destabilizing elongation complexes. Seems to translocate with the RNA polymerase following initiation and acts by binding to the non template strand of the transcription bubble in elongation complexes.
|
Q2FT22
|
Q68XP0
|
DHSD_RICTY
|
Succinate dehydrogenase hydrophobic membrane anchor subunit
|
typhus group
|
MIYDFKAEIIKSKSSSSSKSGAHHWLLQRVTGVVLALCSFWLIYFMFTNKNNDINIIMWEFKKPFNIVILLITVTISLYHSVLGMRVVIEDYINCHKLRNTLIIIVKLFCILTIVAFIVAIFYSE
|
Membrane-anchoring subunit of succinate dehydrogenase (SDH).
|
Q68XP0
|
B9DKG1
|
THIG_STACT
|
Thiazole synthase
|
Staphylococcus
|
MLKIGPYEMESRLLLGTGKFDNEEIQTKAIEASGTDVLTFAVRRMNLYDKNLPNPLANVNLKDFVTFPNTAGAKTVDEAIRIAEIAKHAGVCDMIKVEIIGDDETLLPDPIATYEACEILLERGYIVCPYIAEDVVLAKRLEELGVHAVMPLASPIGTGRGINNPLNLSYIVKNANVPIIVDAGIGSAKDAAEAMELGADAVLLNSAVSRAKDPVKMAEAMKLGIEAGRLSYEAGRIPVKYTAQASSPSEGLGFL
|
Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
|
B9DKG1
|
Q8N5H3
|
LRA25_HUMAN
|
Leucine repeat adapter protein 25
|
Homo
|
MNGLPSAEAPGGAGCALAGLPPLPRGLSGLLNASGGSWRELERVYSQRSRIHDELSRAARAPDGPRHAAGAANAGPAAGPRRPVNLDSALAALRKEMVGLRQLDMSLLCQLWGLYESIQDYKHLCQDLSFCQDLSSSLHSDSSYPPDAGLSDDEEPPDASLPPDPPPLTVPQTHNARDQWLQDAFHISL
|
Negatively regulates TGF-beta-induced signaling; in cooperation with SKI prevents the translocation of SMAD2 from the nucleus to the cytoplasm in response to TGF-beta. Acts as an adapter that mediates the specific recognition of LIMK1 by CDC42BPA and CDC42BPB in the lamellipodia. LRAP25-mediated CDC42BPA/CDC42BPB targeting to LIMK1 and the lamellipodium results in LIMK1 activation and the subsequent phosphorylation of CFL1 which is important for lamellipodial F-actin regulation.
|
Q8N5H3
|
Q65T25
|
GLNE_MANSM
|
Adenylyl transferase
|
Basfia
|
MTMPLPSIEQTLIQLADNLITHFPEQFNSQIYQQIQKDISNIKTPVGALMRAVSMSDFVTEILQKQPHFLAECWHKTPQLADCDSYAARLSVQLADIREETGLYKTLRDFRNQEMAKLSICQSLNSATVEEIFIRLSQLAEALIIGARDWLYQRACLDWGTPTDNQGNVQQLYILGMGKLGGFELNFSSDIDLIFTYPANGETVGSRKPIDNQKFFTRLGQRLISALDEFTEDGFVYRTDMRLRPFGDSGALALSFNAMESYYQEQGRDWERYAMIKGRILGADEQDPNVKTLRQLLRPFIYRRYIDFSVIQSLRDMKSKIEREVLRRGLVDNIKLGAGGIREIEFIVQVFQLIRGGREISLQQHELLKLLPEIEKLNLITADQHQDLLQAYLFLRRVENVLQAINDKQTQLLPADELNRCRLISATCEFTQWDNNHRPQKIQYPIHDWESFYQVLQQHQQKVRSVFNNLIGFNNENEADDSDNAWSDFLDADLEQGEIADILAQQGVSEEERDEIIGRLEAFRHSVSHRSIGIRGREVLTQLMPLLLLQIFSNKKYRTLLPRMLNIVEKILTRTTYLELLLENPQALTQLIELCAKSQLIAEQVAQHPILLDELLDREALLNPPSFEQYPAELQQYLLRLPEDDDEQFITALRQFKQATLLRIAAADILGALPVMKVSDHLTFLAETILHTVVNLAWQQITARFGKPEHLQNNEKGFLVAGYGKLGGIELGYRSDLDLVFLCDEIHSGQTVGGKKVIDSHQFYLRLAQKIISIFSMTTSAGILYEVDLRLRPSGEAGPLCCSFKAFEDYQMNEAWTWEKQSLVRSRAVYGEPALREKFELIRTGILASPRDLTQLKIDVREMREKMYRHFAGADDNKFNIKKDQGGITDIEFIAQYLVLAHAPENPNLAYWSDNVRIFDIMAEHGIITLNEAEKLKNCYTGLRNQIHHLNLLGEPPIVSKEEFADERRFIHQIWQKLFFE
|
Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB) which indicates the nitrogen status of the cell.
|
Q65T25
|
A1TYL6
|
RL15_MARN8
|
50S ribosomal protein L15
|
Marinobacter
|
MRLNELAPEPGSRPSAKRVGRGIGSGLGKTGGRGHKGLKSRSGGSVAPGFEGGQQPLARRLPKFGFTSRQQRYVAEIRLNELAKVEGDVVDLAALKKADIIREEIREAKVILSGELDRAVTVKGLRVTKGAREAITAAGGKVED
|
Binds to the 23S rRNA.
|
A1TYL6
|
Q8KWS9
|
BACC_BACAM
|
Bacilysin biosynthesis oxidoreductase BacC
|
Bacillus amyloliquefaciens group
|
MNLTDKTVLITGGASGIGYAAVQAFLNQQANVVVADIDEAQGEAMIRKENNDRLHFVQTDITNEPACQNAILSAVDKFGGLDVLINNAGIEIVAPIHEMELSDWNKVLNVNLTGMFLMSKHALKYMLKSGKGNIINTCSVGGVVAWPDIPAYNASKGGVLQTDAFYRPSIIAKHNIRVNCVCPGIIDTPLNEKSFLENNEGTLEEIKKEKAKVNPLLRLGKPEEIANVMLFLASDLSSYMTGSAITADGGYTAQ
|
Part of the bacABCDEFG operon responsible for the biosynthesis of bacilysin, an irreversible inactivator of the glutaminase domain of glucosamine synthetase. Catalyzes the dehydrogenation of the C7-hydroxyl group in the 4S-tetrahydrotyrosine (4S-H4Tyr) to yield anticapsin (epoxycyclohexanonyl-Ala).
|
Q8KWS9
|
Q30NW9
|
LSPA_SULDN
|
Signal peptidase II
|
Sulfurimonas
|
MHNKTVRHLTILILTIAGIFIIDQNIKSLFVDGYRYYSDCIDLILVYNKGVAFSMFAFLDESLKYIQLVLVFGVFGYMLYLNQLCYAIPAGLMLGGAFSNIYDRFIHGGVVDMVYWHCGFDFAVFNFADVMIDVAVVWILLLNFKPKFCKNHS
|
This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
|
Q30NW9
|
B7LS90
|
AROB_ESCF3
|
3-dehydroquinate synthase
|
Escherichia
|
MERITVTLGERSYPITIAAGLFNEPASFLPLKSGEQVMLVTNETLAPLYLDKVRGVLEQAGVIVDSVILPDGEKYKSLTVLDTVFTALLQKPHGRDTTLVALGGGVIGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPASVVVDLDCLQTLPARELASGLAEVIKYGIILDGEFFTWLEENLDALLRLDGPAMAYCIRRCCELKAEVVAADERETGLRALLNLGHTFGHAIEAEMGYGNWLHGEAVAAGMVMAARTSERLEQFSSADTQRIIALLERAGLPVNGPREMSAEAYLPHMLRDKKVLAGEMRLVLPLALGKSEVRGGVPHDVVLSAIADCQQA
|
Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
|
B7LS90
|
A4SCU5
|
BCHB_CHLPM
|
Light-independent protochlorophyllide reductase subunit B
|
Chlorobium
|
MRLAFWLYEGTALHGISRITNSMKGVHTVYHAPQGDDYITATYTMLERTPEFPALSISVVRGRDLAQGVSRLPATLQQVEHHYHPELTVIAPSCSTALLQEDLRQLAAHSGVAQEKLMVYAVNPFRVTENEAADGLFTELVKRYAANGQKSAVPAVNLLGFTSLGFHLKANLTSLRRMLSTLGVKVNVVAPWGAGIADLARLPEAWLNIAPYHEIGRTAAEYLEQEFAMPAVYDTPIGVEPTLRWLRSIIEKLNEVGAGCGASPISMPALHDFSLDGMSAPSGVPWFARTADMESFSNKKAFVFADATTTVAMVKFLRDELGMKVVGAGTYLERDADWVRRELEGYLPGELMVTDRFQDVAKVIEDELPDLVCGTQMERHSCRKLDIPCMVVSPPTHIENHLLGYYPFFGFDGADVIADRVYLSCKLGLEKHLIDFFGDAGLEYEDGDAADETGVAAAAANGHSPAGGSTEGEGGMVWTGEAETMLKKVPFFVRKKVRKNTETFAMEQGEGEVTVEVFRRAKDSLGG
|
Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (BchN-BchB) is the catalytic component of the complex.
|
A4SCU5
|
B1KSN2
|
RPOC_CLOBM
|
Transcriptase subunit beta'
|
Clostridium
|
MFELNNFDALQIGLASPEKIREWSRGEVKKPETINYRTLKPERDGLFCERIFGPMKDWECHCGKYKRIRYKGIVCDRCGVEVTKAKVRRERMGHIELAAPVSHIWYFKGIPSRMGLILDMSPRALEKVLYFASYVVLDPKETPLLKKQLLNEKEYRESIDKYGDDSFVAAMGAEAVKTLLDEIDLEQSSIELKEELKTSTGQKKIRIIRRLEVVESFRKSGNRPDWMVIDVIPVIPPDLRPMVQLDGGRFATSDLNDLYRRVINRNNRLKKLLDLGAPDIIVRNEKRMLQEAVDALIDNGRRGRPVTGPGNRPLKSLSDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPELKMYQCGLPKEMALELFKPFVMKKLVQNGLAHNIKSAKRMVERVQPQVWDVLEEVISDHPVLLNRAPTLHRLGIQAFQPVLVEGRAIKLHPLVCTAYNADFDGDQMAVHVPLSVEAQAEARFLMLAAHNILKPSDGKPVSVPTQDMVLGSYYLTMDKDGVKGEGKVFSCPEEVLMAYQCKAVDIHAKIKVRLKRVVDGETIEGIIETTPGKIIFNESIPQDLGYIDRTIPENKLKLEVDFLVSKKTLGGIITRCYMKHGATKTSIMLDKIKAKGYHYSTIGAITISTSDMVVPEAKRELLENTEKQVEKIQKMYRRGFISEEERYEKVIDLWTKTTEDVANALMGSLDSFNPIYMMADSGARGSKSQIKQLAGMRGLMANPSGKIIELPIKASFREGLDVLEYFISTHGARKGNADTALKTADSGYLTRRLVDVSQDVIVRQEDCGTEEGYEVSEIKEGNEVIEPLVERLSGRYPSEDIIHPTTGEVIVKRNTYMNEDIAKKVSDAGIKKVKIRSVFTCKSKHGVCARCYGMNMATSQKIHIGEAVGIVAAQSIGEPGTQLTMRTFHTGGVAGADITQGLPRVEELFEARKPKGLAIVSEVSGTVKMEETKKKRTIIVVTDDGEEVSYDIPFGSRIKVKNGDIIAAGDEITEGSINPHDILRIKGVDGVKNYLLSEVQKVYRLQGVDINDKHLEVVIRQMTRKIKIEDSGDTELLPGTMIDVFDFEEANKEILEKGGEPAVGRIALLGITKAALATDSFLSAASFQETTRVLTDAAIKGKIDPLLGLKENVIIGKLIPAGTGMTRYRSIQINTDDENIEEDSIDSIEV
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
B1KSN2
|
P07231
|
CKG_CONGE
|
Sleeper peptide
|
Gastridium
|
MHLYTYLYLLVPLVTFHLILGTGTLDDGGALTERRSADATALKAEPVLLQKSAARSTDDNGKDRLTQMKRILKQRGNKARGEEELQENQELIREKSNGKR
|
Conantokins inhibit N-methyl-D-aspartate (NMDA) receptors. This toxin is selective for the NR2B/GRIN2B subunit. Induces sleep-like symptoms in young mice and hyperactivity in older mice.
|
P07231
|
Q88CT0
|
IXTPA_PSEPK
|
Nucleoside-triphosphate pyrophosphatase
|
Pseudomonas
|
MMNFQQLVLASHNAGKLKELQAMLGHSVQLHSIGEFSQVEPEETGLSFVENAILKARNAARISGLPALADDSGLAVDFLGGAPGIYSARYADGKGDAANNAKLLEALKDVPEAERSAQFVCVLALVRHADDPLPILCEGLWHGRILFEASGDQGFGYDPLFWVPERNCSSADLAPADKNQLSHRARAMALLRKRLGLA
|
Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
|
Q88CT0
|
B6JBH5
|
FLGH_AFIC5
|
Basal body L-ring protein
|
Afipia
|
MSRLRTSHALRTAAALVAVGCLASGCSSIERLSQIGEQPKLTAIDNPTTKAGYKPVSMPMPTPQPASYNPNSLWRNGSRAFFKDQRAHQVGDILTVIVNITDKANIANETQRSRANTEDSSITNFFGIKKVPGTNGAGNMLTTGSVASSDGKGSVVRQEALQTNVAAVVTQLLPNGNLVVEGKQEIRVNFEMRELVVAGIVRPEDIQSDNTIDSSKIAQARIAYGGRGQITDVQQPRYGQQVMDILLPF
|
Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
|
B6JBH5
|
P46953
|
3HAO_RAT
|
3-hydroxyanthranilic acid dioxygenase
|
Rattus
|
MERCVRVKSWVEENRASFQPPVCNKLMHREQLKIMFVGGPNTRKDYHIEEGEEVFYQLEGDMVLRVLEQGEHRDVVIRQGEIFLLPARVPHSPQRFANTMGLVIERRRMETELDGLRYYVGDTEDVLFEKWFHCKDLGTQLAPIIQEFFHSEQYRTGKPNPDQLLKEPPFPLSTRSVMEPMSLKAWLESHSRELQAGTSLSLFGDSYETQVIAHGQGSSKGPRQDVDVWLWQLEGSSKVTMGGQCVALAPDDSLLVPAGFSYMWERAQGSVALSVTQDPACKKPLG
|
Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
|
P46953
|
Q8XJ42
|
SYV_CLOPE
|
Valyl-tRNA synthetase
|
Clostridium
|
MDNKNISTTYNPKEFEERLYSNWQEKKYFTPVIDKSKKPYTIIMPPPNITGKLHLGHALDNTLQDMLIRFKRMQGYCTLWLPGQDHASIATEVKVENELLKEGLYKKEMGREAFLEKVWEWTDEYRERIREQLKKMGCSADFTREAFTMDENLSKAVRHVFVKLYKEGLIYQGNRITNWCPKCQTALSDAEIEYEEKEGNFWHIKYPVVGSEEFLEIATTRPETLLGDSAVAVNPSDERYAHLVGKMLKLPLTDREIPVIADDYVDVEFGTGAVKITPAHDPNDFEVGKRHNLPQIRVMDDSGVINHLGGKYKGLDRYEARKQMVADLEELGLLVKIKPHTHNVGTHDRCGTVVEPIISKQWYVKMQSLADPAIEVVRNKGTKFVPERFEKTYFNWMENIQDWCISRQLWWGHRIPVFYCKDCGEIMVELEDPTKCCKCGSENIEQDKDVLDTWFSSALWPFSTLGWPDRTDDLEFFYPTSTLVTGYDIIFFWVARMIFSGIHNMGETPFDTVLIHGIIRDAQGRKMSKSLGNGVDPLEVIDEYGADALRFMLVTGNAPGNDIRYIPERVEAARNFANKIWNASRFVMMNLDRELMDKYKDCQEYSLADQWILSRTNSLIKEVTENMEKYELGIALQKVHDFLWTEFCDYYIELVKPVLYGDDEKAKGVVFNVLYTVLNTGLKLLHPVMPFITEEIYTHLSTETESITIATWPTYDEALNNEKAEKDMTFIMEAIRSLRNLRAEMNVPPSRKAKVMAYASEEAKDAFINGGAYLEKLASASEVTFLDNKDNLDNNLVSVVVKGGELFLPLLDLVDREKELERLNKEKTKLEGEILRVEKKLSNERFVSKAPEAVVNEERAKGVKYKEMLEAVLERIEALQ
|
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.
|
Q8XJ42
|
C1ESK7
|
DNAJ_BACC3
|
Chaperone protein DnaJ
|
Bacillus cereus group
|
MSKRDYYEVLGLSKGASKDEIKKAYRRLAKKYHPDVSKEENAIEKFKEVQEAYEVLSDDQKRAQYDQFGHAGANQGFGGFGGGGDFGGGFGFEDIFSSFFGGGGGRRRDPNAPRQGADLQYQVTLDFEEAIFGKELNVEIPVEDPCDTCKGSGAKPGTSKETCKHCSGSGQVSVEQNTPFGRIVNRQACSHCSGTGQMIKEKCTTCHGSGKVRKRKKINVKIPAGIDNGQQIRVSGKGEAGVNGGPAGDLYVVVHVRSHEFFEREGDHIICEMPLTFAQMALGAEVEVPTVHGKVKLKIPAGTQTGTEFRLKGKGAPNVRGYGQGDQYVVVRVVVPTKLTSHQKDLLREFAGQEEQDDSLFGKLKRAFKGE
|
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
|
C1ESK7
|
Q06407
|
RGA2_YEAST
|
Rho-type GTPase-activating protein 2
|
Saccharomyces
|
MSADPINDQSSLCVRCNKSIASSQVYELESKKWHDQCFTCYKCDKKLNADSDFLVLDIGTLICYDCSDKCTNCGDKIDDTAIILPSSNEAYCSNCFRCCRCSNRIKNLKYAKTKRGLCCMDCHEKLLRKKQLLLENQTKNSSKEDFPIKLPERSVKRPLSPTRINGKSDVSTNNTAISKNLVSSNEDQQLTPQVLVSQERDESSLNDNNDNDNSKDREETSSHARTVSIDDILNSTLEHDSNSIEEQSLVDNEDYINKMGEDVTYRLLKPQRANRDSIVVKDPRIPNSNSNANRFFSIYDKEETDKDDTDNKENEIIVNTPRNSTDKITSPLNSPMAVQMNEEVEPPHGLALTLSEATKENNKSSQGIQTSTSKSMNHVSPITRTDTVEMKTSTSSSTLRLSDNGSFSRPQTADNLLPHKKVAPSPNKKLSRSFSLKSKNFVHNLKSKTSEMLDPKHPHHSTSIQESDTHSGWGVSSTHTNIRKSKAKKNPVSRGQSDSTIYNTLPQHGNFTVPEFNHKKAQSSLGSISKKQNSNDTATNRRINGSFTSSSSGHHIAMFRTPPLESGPLFKRPSLSSESAHHRSSSLQTSRSTNALLEDDSTKVDATDESATSLEKDFYFTELTLRKLKLDVRELEGTKKKLLQDVENLRLAKERLLNDVDNLTREKDKQSASSRESLEQKENIATSITVKSPSSNSDRKGSISNASPKPRFWKIFSSAKDHQVGDLESQQRSPNSSSGGTTNIAQKEISSPKLIRVHDELPSPGKVPLSPSPKRLDYTPDGSHLYGSSLQARCAYEKSTVPIIIRCCIDRIEKDDIGLNMEGLYRKSGSQTLVEEIENEFAQNNSLHSDTLSPKLNALLNQDIHAVASVLKRYLRKLPDPVLSFSIYDALIDLVRNNQLIERLPLNNDKFLDSPQKVTIYEMVLKSLLEIFKILPVEHQEVLKVLAAHIGKVRRCSERNLMNLHNLSLVFAPSLIHDFDGEKDIVDMKERNYIVEFILGNYRDIFKQA
|
GTPase-activating protein (GAP) for CDC42 and/or RHO1.
|
Q06407
|
B2J183
|
RSMH_NOSP7
|
rRNA (cytosine-N(4)-)-methyltransferase RsmH
|
Nostoc
|
MKSDLETPLNLEELAFSHISVLGREVIEGLAVRPGGHYLDVTVGGGGHSRLILEAAADVRVTAVDQDEDALVAANKNLAEYSDRIQFIYSNFADYEFPPNTFDGILADLGVSSYHLDQAERGFSFRQAANLDMRMDRGRSLTAADVINNWDEAELADIFFKYGEERLSRRIARRIVERRPLHTTTELADAIASSVPPKYRYGRIHPATRVFQALRIVVNDELKSLETFLDKAPNALVPGGRIAIISFHSLEDRPVKHGLRNSPLLKVLTKKPIIAQEEEISNNPRSRSAKLRIAEKLV
|
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
|
B2J183
|
A0M3K8
|
RIMO_GRAFK
|
Ribosome maturation factor RimO
|
Gramella
|
MRTKSLKKNRINVVTLGCSKNVYDSEILMGQLKANDKDVVHEEDGNIVVINTCGFIDNAKEQSVNTILEFVEKKQQGDVDKVFVTGCLSERYKPDLQKEIPDVDQYFGTTELPGLLSALEADYKHELIGERLTTTPKNYAYLKIAEGCDRPCSFCAIPLMRGGHKSTPIENLVTEAEKLAANGVKELILIAQDLTYYGLDLYKKRNLAELLENLVKVEGIEWIRLHYAFPTGFPMDVLEVMKREPKVCNYLDIPLQHISDDLLKSMRRGTTHEKTTKLLKEFRKTVPEMAIRTTLIVGYPGETEEHYQELKEWVKEMRFERLGCFTYSHEENTHAYNLEDDVPQEVKQERANEIMEIQSQISWELNQQKIGEVFNVVIDRKEGNYFIGRTEYDSPDVDNEVLIDATTVYLKTGDYYDVKIAEAADFDLYGEPLNVTTEKPKRKELKIKSV
|
Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12.
|
A0M3K8
|
A4W3Q2
|
RS6_STRS2
|
30S ribosomal protein S6
|
Streptococcus
|
MAKYEILYIIRPNIEEEAKNALVARFDSILTDNGATIVESKAWEKRRLAYEIKDFREGLYHIVNVEANNDEALKEFDRLSKINGDILRHMIVKLDA
|
Binds together with S18 to 16S ribosomal RNA.
|
A4W3Q2
|
O65976
|
BLC6_SALTM
|
Cefotaximase 6
|
Salmonella
|
MMTQSIRRSMLTVMATLPLLFSSATLHAQANSVQQQLEALEKSSGGRLGVALINTADNSQILYVADERFAMCSTSKVMAAAAVLKQSESDKHLLNQRVEIRASDLVNYNPIAEKHVNGTMTLAQLGAGALQYSDNTAMNKLIAHLGGPDKVTAFARSLGDETFRLDRTEPTLNSAIPGDPRDTTTPLAMAQTLKNLTLGKALAETQRAQLVTWLKGNTTGSASIRAGLPKSWGVGDKTGSGDYGTTNDIAVIWPENHAPLVLVTYFTQPEQKAESRRDVLAAAAKIVTHGF
|
Has cefotaxime-hydrolyzing activity.
|
O65976
|
P53137
|
CUE3_YEAST
|
Coupling of ubiquitin conjugation to ER degradation protein 3
|
Saccharomyces
|
MLSRYNRVIEINGGNADISLPIVKFPPFKLRAQLIEKDPVVWLHLIETYVTYFEYLMQGANVELLDESTLDHLRLFLRTYLHEIADEEGKLLSLGINHDVSEQLYLLKGWIFSLIKKCGLLHLQIFGDSLWNLIKVYVRRNPDSIRGLIDGSLKPRINTQRVQLDKSYQVQQHLKQLIESGKFKRIDLRCVEDLLSAKSMQPNKFAENFFTANWIEILEALWAKGQGRGHKEARELIIISLFSVSADRLLKITKELGISNFETLALYPLLGTMLINEGVHKRLPDLKSKLLFLNLGGLSMDEGDHMSYPTSSGTEVNEEQLSALMELFPQFSKYQLSQTLLAYDNNIELVTNKIFEDPTIIEAFSREPAEEEVEPVSDGDNASFTEELSILDRGDSSKNKELDKKIISEGVPDELRNKTLTRALKLLYEADEDERDDTYDEADVNRSDPSKRIGLQEDEESYDTKDDSNEVRQDHNYHIVEAYLWNLLKEDPKLFERSKRGTKVRKTMKEMTSWSDEKIEGWCRMLERSPTRARLLEKKFMFKGNSKTGKTSYVHNRDSQNDGNVVKEQAKQKKSENIKKHEPQSTEQKKRQHAKNEKRKGARANHNRKKGHDKKLARAGNNAI
|
Involved in activation of the ribosome quality control (RQC) pathway, a pathway that degrades nascent peptide chains during problematic translation . As part of the ribosome quality control trigger (RQT) complex, recognizes HEL2-dependent ubiquitination of RPS20 on stalled ribosomes .
|
P53137
|
A4WF38
|
NANA_ENT38
|
Sialic acid lyase
|
Enterobacter
|
MAKQLRGVMAALLTPFNTQQALDKESLRRLVQFNMQQGIDGLYVGGSTGEAFVQSLSEREQVLEIVAEEAKGKITLIAHVGCVSTAESQQLAASASRFGFDAVSAVTPFYYPFSFEEHCDHYRAIIDSADGLPMVVYNIPALSGVKLTLDQINTLVTLPGVGALKQTSGDLFQMEQIRRAHPDLVLYNGYDEIFASGLLAGADGGIGSTYNIMGWRYQAIAKAIREGDNATAQRLQSECNKVIDLLIKVGVFRGLKTVLHYMDVVSVPLCRKPFAPVAEPYLPELKALAKQLMVEKA
|
Catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine (ManNAc) via a Schiff base intermediate.
|
A4WF38
|
A5WCX3
|
EFTS_PSYWF
|
Elongation factor Ts
|
Psychrobacter
|
MSKISAKLVKELRDRTGLGMMECKKALEETNGDVEQAIDNLRKSGQAKAAKKAGNIAADGAIVIAQEGNKAILLEVNCQTDFVAKDDNFTEFANKVAELALANNTTDVAAISELDYGNGQSVEEARVALVQKIGENIQVRRAKIIEGDNLASYRHGLRIGVVVSSEGGQEDSGKNLAMHIAAFNPVAVNDTDVPADILAREKDIAEAKARESGKPDNIIEKMIEGGLRKYLDEVVLVRQAYVMDNEKKVGDVLKADGVTVKDFVRFEVGEGIEKKQEDFAAEVAAAQAAAAQ
|
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
|
A5WCX3
|
Q8FHD2
|
YDFG_ECOL6
|
Malonic semialdehyde reductase
|
Escherichia
|
MIVLVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMLASLPAEWSNIDILVNNAGLALGMEPAHKASIEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSWPYAGGNVYGATKAFVRQFSLNLRTDLHGTAVRVTDIEPGLVGGTEFSNVRFKGDDGKAEKTYQNTVALTPEDVSEAVWWVSTLPAHVNINTLEMMPVTQSYAGLNVHRQ
|
NADP-dependent dehydrogenase with broad substrate specificity acting on 3-hydroxy acids. Catalyzes the NADP-dependent oxidation of L-allo-threonine to L-2-amino-3-keto-butyrate, which is spontaneously decarboxylated into aminoacetone. Also acts on D-threonine, L-serine, D-serine, D-3-hydroxyisobutyrate, L-3-hydroxyisobutyrate, D-glycerate and L-glycerate. Able to catalyze the reduction of the malonic semialdehyde to 3-hydroxypropionic acid. YdfG is apparently supplementing RutE, the presumed malonic semialdehyde reductase involved in pyrimidine degradation since both are able to detoxify malonic semialdehyde.
|
Q8FHD2
|
Q18DH5
|
BACRM_HALWD
|
Middle rhodopsin
|
Haloquadratum
|
MATPGSEATWLWIGTIGMVLGTVYFAVRGRGSTDPEQQTYYIITTLIPAIAAAAYLAMATGLGVISMPIRGTEVIDIYWARYADWLLTTPLLIIDLALVAGARKQTLYKLIIIDAIMILGGLAGSMMQQGAVIRIVWWAVSTAAFIILLYYLLGELSERARSRSAETGIVFNRLRNITLGLWALYPIVWILGTGGGFGIIAVTTEIMLYVMLDIGTKIGFGAVLLESQDVLQAASHPSSTNDIKSH
|
Has no proton-pumping activity but is potentially capable of functioning as a sensory SRII-like protein. The chromophore contains 36.5% all-trans-, 7.6% 11-cis- and 56.4% 13-cis-retinal in the dark and 30.1% 11-cis- and 47.7% 13-cis-retinal upon illumination with >460 nm light.
|
Q18DH5
|
B7L916
|
COBT_ECO55
|
N(1)-alpha-phosphoribosyltransferase
|
Escherichia
|
MQTLADLLNTIPAIDPAAMSRAQRHIDGLLKPVGSLGRLEALAIQLAGMPGLNGIPHVGKKAVLVMCADHGVWEEGVAISPKEVTAIQAENMTRGTTGVCVLATQAGANVHVVDVGIDSAEPIPGLINMRVARGSGNIASAPAMSRRQAEKLLLDVICYTRELAKNGVTLFGVGELGMANTTPAAAIVSTITGRDPEEVVGIGANLPTDKLANKIDVVRRAITLNQPNPQDGVDVLAKVGGFDLVGMAGVMLGAASCGLPVLLDGFLSYAAALAACQMSPAIKQYLIPSHLSAEKGARIALSHLGLEPYLNMEMRLGEGSGAALAMPIIEAACAIYNNMGELAASNIVLPGNTTSDLNS
|
Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
|
B7L916
|
Q6IN84
|
MRM1_HUMAN
|
16S rRNA [Gm1145] 2'-O-methyltransferase
|
Homo
|
MALLSTVRGATWGRLVTRHFSHAARHGERPGGEELSRLLLDDLVPTSRLELLFGMTPCLLALQAARRSVARLLLQAGKAGLQGKRAELLRMAEARDIPVLRPRRQKLDTMCRYQVHQGVCMEVSPLRPRPWREAGEASPGDDPQQLWLVLDGIQDPRNFGAVLRSAHFLGVDKVITSRRNSCPLTPVVSKSSAGAMEVMDVFSTDDLTGFLQTKAQQGWLVAGTVGCPSTEDPQSSEIPIMSCLEFLWERPTLLVLGNEGSGLSQEVQASCQLLLTILPRRQLPPGLESLNVSVAAGILLHSICSQRKGFPTEGERRQLLQDPQEPSARSEGLSMAQHPGLSSGPEKERQNEG
|
S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methylguanosine at position 1145 (Gm1145) in the 16S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA.
|
Q6IN84
|
Q3SPI3
|
LPXK_NITWN
|
Lipid A 4'-kinase
|
Nitrobacter
|
MREPAFWRRPSSLLSRLLIPVGALYGAIAARRLSRTGLRAGVPVICVGNYHLGGAGKTPTVLALAGILRSLGETPVVISRGYGGRLRGPVRVDPDRHAAADVGDEPLMMARTLPVIVSRQRAAGVAPARALGASVILMDDGFQNPTLARDISLIVIDGDRGLGNRRIFPAGPLRAPLPPQLARTDALVIVGPGSAADDIAASIEARGGPVLRARVVPDEASVAALRGRRVLAFAGIGDPSRFFRGLRACGVDVAAERAFADHHPFSQRDVAALQSAAEKDGLTLVTTEKDLARLRNNENIAAFAQAVAPFAVTLAFDDETALRSFLMDGIAKVRRLD
|
Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
|
Q3SPI3
|
Q81HT3
|
QOX2_BACCR
|
Quinol oxidase polypeptide II
|
Bacillus cereus group
|
MQLKKAFWKLASLLPLSLLLFLGGCDKKLAVLNPQGPVAKAQYDLIVWSFLLMSLIIAIVFILFTVILIRYREKPENMDYEPPEQHGNTLLEIIWTLVPVIIVIALSIPTVKATYASEEVPKESKHIKPVEIYVTSANWKWLFSYPEEKIETVNYLNIPAGVPIQFKLTSVGPMNAFWVPELGGMKYTMDGMIMDLYLQADKPGSYLGRSANFSGEGFTHMEFEVEAKTKEKYDKWVKEVQETAPKLTEAKYNEIVKPGVVGRMTFSSHHLSYVDPKSLEYCDYNYYKNKK
|
Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Subunit II transfers the electrons from a quinol to the binuclear center of the catalytic subunit I.
|
Q81HT3
|
Q9ATM5
|
PIP26_MAIZE
|
ZmPIP2;6
|
Zea
|
MGKEVDVSTLEAGGVRDRDYADPPPAPLIDIDELGKWSLYRAVIAEFVATLLFLYITVATVIGYKHQTDASASGPDAACSGVGILGIAWAFGGMIFILVYCTAGISGGHINPAVTFGLFLARKVSLVRALLYMAAQSLGAICGVALVKGFQSGFYARYGGGANEVSAGYSTGTGLAAEIIGTFVLVYTVFSATDPKRNARDSHVPVLAPLPIGFAVFMVHLATIPITGTGINPARSLGAAVVYNNSKAWSDQWIFWVGPFIGAAIAALYHQIVLRASARGYGSFRSNA
|
Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.
|
Q9ATM5
|
A5EWL8
|
DEF_DICNV
|
Polypeptide deformylase
|
Dichelobacter
|
MAIYSILIHPDPRLRLPAQPVTHFDDALAEIVQNMYETMYHFHGIGLAAPQVNIQQRLIVMDVPQRSAEEGEKAEQIPSDKLVLVNPEIVQRSEECQDYEEGCLSLPNQYALVTRPANITVRYQDITGATQERAAQGLLSVCIQHEIDHLNGGLFIDHLSRLKRERLEKKLAKSLKNTKKS
|
Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
|
A5EWL8
|
A1REB4
|
RL3_SHESW
|
50S ribosomal protein L3
|
Shewanella
|
MAIGLIGRKVGMTRIFTEDGVSIPVTVIEVAGNRVTQVKTLETDGYRALQVTTGTKKANRITKPEAGHFAKSGVEAGRGLWEVRLEDGEGEGIEVGAELNVDIFADVAKVDVTGQSKGKGFQGGVKRWNFRTQDMTHGNSLSHRSNGSIGQNQTPGRVFKGKKMSGHMGAERVTTQNLVVVRVDVERNLLLVRGAVPGATNGDLIIKPAVKA
|
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.
|
A1REB4
|
Q9PK47
|
XERC_CHLMU
|
Tyrosine recombinase XerC
|
Chlamydia
|
MIASFYAFLDYLKNMKAASPHTLRNYSIDLSSLKCFLEKKGELTPTPPLSLQEDSRSSSQLSFSLFTKENIRLYLLEQIQTTHSKRTVRRRLSAIKSFAKFCVKNQWIPENPAEMIRGPRLPKELPSPLTYEQVLALMSAPDLDKVTGFRDRCLLELFYSSGLRISEITALNRSDIDFQSNLLRICGKGKKERIVPMTKVAVQWLQAYLDHPDRAAVEQDHQACFLNRFGKRLSTRSIDRKFQQYLLKTGLSGTITPHTIRHTIATHWLERGMDLKTIQLLLGHTSLETTTIYTHVSMKLKKQIHDEAHPHNLED
|
Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC-XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids.
|
Q9PK47
|
A6T0T5
|
NRDR_JANMA
|
Transcriptional repressor NrdR
|
Janthinobacterium
|
MKCPFCQHDDTQVLDTRVSEEGDSIRRRRRCTSCDKRFTTYERIELTMPVVVKKNGSRTDFDPKKLQGSLQLALRKRPVSAEAVDAAIHRIEQKLLSSGEREVISGQIGELVMRELQRLDKIAYIRFASVYKSFEDVAEFQDAIAEVGRERKPAK
|
Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
|
A6T0T5
|
Q06H09
|
ATPI_DRIGR
|
F-ATPase subunit IV
|
Drimys
|
MNVLPCSINTLKGLYDLSGVEVGQHFYWQIGGFQVHAQVLITSWVVIAILLGSATIAVRNPQTIPTKSQNFFEYVLEFIRDLSKTQIGEDYGPWVPFIGTMFLFIFVSNWSGALLPRKIVQLPHGELAAPTNDINTTVALALPTSVAYFYAGLTKKGLGYFGKYIQPTPILLPINILEDFTKPLSLSFRLFGNILADELVVVVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIGESMEGHH
|
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
|
Q06H09
|
Q0TC10
|
UGPC_ECOL5
|
sn-glycerol-3-phosphate import ATP-binding protein UgpC
|
Escherichia
|
MAGLKLQAVTKSWDGKTQVIKPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTTGDIWIDRKRVTEMEPKDRGIAMVFQNYALYPHMSVEENMAWGLKIRGMGKQQIAERVKEAARILELDGLLKRRPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLELQQLHRRLKTTSLYVTHDQVEAMTLAQRVMVMNGGVAEQIGTPVEVYEKPASLFVASFIGSPAMNLLAGRVNNEGTHFELDGGITLLLNGGYRQYAGRKMTLGIRPEHIALSSRAEGGVPLVMDTLEILGADNLAHGRWGEQKLVVRLAHQERPTAGSTLWLHLPENQLHLFDGETGQRV
|
Part of the ABC transporter complex UgpABCE involved in sn-glycerol-3-phosphate import. Responsible for energy coupling to the transport system.
|
Q0TC10
|
Q2U2I3
|
MANF_ASPOR
|
Endo-beta-1,4-mannanase F
|
Aspergillus subgen. Circumdati
|
MRSLSSIALLSVVGAASAQAGPWAQCGGKSFSGSSECASGWKCQELNEWFSQCVPGAESTTPTVSSTPTPTDAPSVSITASVTTGINKSISVSSASKSTPLPSSSSASPSPRPTGSGSFAKADGLQFSIDGETKYFAGTNAYWLPFQMNDADIDSVFDHLEQAGLKILRVWGFNDVNTAPSPGTVYFQLHDKEKGTSTINTGKDGLQRLDYVVAAAEKHGVKLIIPFVNSWDDYGGYNAYVKAYGGSKTEWFTNEKIQSVYQAYIKAVVSRYRDSPAIFAWELGNEPRCSGCSTDVIHGWATKISAYIKSLDPNHMVALGDEGMGLTIGSDQSYPYGTSEGNDFEKNLAIPDIDFGTLHLYTTDWGIKDNAWGNGWVENHAKACKAAGKPCLFEEYGMKGNHCTDELKWQKTSLSSGTAADLIWQYGQQLSTGESPKDAYSIFYGTDEWKCAVMDHMENVNKN
|
Endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans.
|
Q2U2I3
|
Q1GX86
|
PRMA_METFK
|
Ribosomal protein L11 methyltransferase
|
Methylobacillus
|
MAWISLRIDARDDNAELLSDTLMELGALSASIEDANAETPDEQPIFGEPGDPPPGIWQQNVVTALLDESADLDSLLEELSAATGITDFRYSTETIAEQDWVRATQSQFEPIRIRDDLWIVPSWHDAPNPDGLNIVLDPGLAFGTGSHPTTHLCLSWLADTVKPDTSVLDYGCGSGILAIAARKLGAGKVVGVDIDAQAIQSSVYNADQNQVDASFYLASDLPGGQFDIVVANILSSALSVLAPALARAARSGGRIALSGILREQADQVSAIYQEWFEMDAPVFMDSWVLLTGSRR
|
Methylates ribosomal protein L11.
|
Q1GX86
|
Q4P5U1
|
JHD1_USTMA
|
[Histone-H3]-lysine-36 demethylase 1
|
Ustilago
|
MTAVAASSRVSDPLAASSSAHPRTLRSSPRKRTTSHDSSISPSAAQSKQLPRRKKPRTELVDESELDCAACPAVGQPAPTPGKGAASDRETWICCTHCKTWFHCICIGLENPDDFSKWYCQPCITRSEQTFESGTSSSHPPFANVVRPPRRKSERAKLQIDYAAIQEGIPADPLGRWKNLLNAYEFEPDQFRRMQGHEWTFDWLLHDESALKQPVLVPAPPDRSSQAPHVQAKAEDVAASPVPRPKPARAKKQATHRLVPCHTSIPGMVVPPPEMSIFDVADIIGHDTPVEVIDVASQSSSKASWTISEWAEYFNTPKEKKKKTLNVISLEVTGTPMQAYVEAPQLVRDLDWVTRDWPAERRDASCSENSWPKVQRYVLMGVEGAYSDWHIDFAGSSVYYHVIWGQKTFLFAPPTARNLAAYKAWCSSTRQDFDWLGDHLHSLTRVDIGPGETMLIPSGWLHCVYTPKNTLVVGGNFLTDWNVATQWKLVEIEEATKVPRKFRFPHLKRLSWFVAKGWNDRLEPLAEFETLTKEEDQVLEESAQVSAQVDVGSLTEVVPPLKVLNNIELVLQSLSDDLELIQDPYVAESGDERKVKQQKAAREAIPTHHVGNIQKAEAMLASLRQRVDRAKSLADAVQSERVCLTWEATRAKKAKAANGSAIKSRKARR
|
Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code.
|
Q4P5U1
|
Q82XY4
|
DAPE_NITEU
|
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase
|
Nitrosomonas
|
MSNSTLTLAQMLIARRSLTPDDDGCQKMIMHRLAGLGFKSDSMTFGEVENLWTRKGSDAPLVCFAGHTDVVPTGPVTQWDSDPFTPVVRDGFLYGRGAADMKTSLAAFVTAIEEFIELHPDHKGSIALLITSDEEGPAVDGTVKVVEALQTRGEMIDYCIVGEPTCTNQLGDTIKNGRRGSLSGNLTVRGIQGHIAYPHLARNPIHTAAPAIAELAQTVWDNGNEYFPATTWHISNIHGGTGATNVIPGEINLLFNFRFSTASTVDSLKARVHEILDRHGLDYELIWELSGKPYLTPRGTLADAVSAAIREVTGIEPELSTTGGTSDGRFIADICQQVVEFGPRNATIHKINESVEVADVERLARIYRLTLENLLL
|
Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls.
|
Q82XY4
|
Q390Z5
|
1A1D_BURL3
|
1-aminocyclopropane-1-carboxylate deaminase
|
Burkholderia cepacia complex
|
MNLQRFPRYPLTFGPTPIQPLKRLSEHLGGKVELYAKREDCNSGLAFGGNKTRKLEYLVPDALEQGADTLVSIGGVQSNQTRQVAAVAAHLGMKCVLVQEHWVNYEDPVYDRVGNIQLSRMMGADVRLVSDGFDIGIRRSWEEAMESVRQAGGKPYPIPAGCSEHPLGGLGFVGFAEEVRAQEAQLGFKFDYIVVCSVTGSTQAGMVVGFAADGRANRVIGIDASATPERTHEQITRIARHTAELVDLGRPITTADVVLDTRYAGPEYGLPNDGTLEAIRLCARLEGMLTDPVYEGKSMHGMIDKVQLGEFEPGSKVLYAHLGGVPALSAYHETFRNG
|
Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate. Allows growth on ACC as a nitrogen source.
|
Q390Z5
|
A8FP64
|
PEPQ_SHESH
|
Proline dipeptidase
|
Shewanella
|
MDQLTNHFHAHVAELNRRVAEIVARENLSGLVIHSGQPHRQFLDDMDYPFKVNPHFKAWLPILDNPHCWLLVNGRDKPQLIFYRPVDFWHKVADLPDEFWTAHVDIKLLTKADKVADLLPKDIVDWAYVGEHLDVAEVLGFKTRNPDAVMSYLHYHRATKTEYELACMRKSNEIAVKGHVAAKNAFYNGGSEFEIQQQYLMATNQGENEVPYGNIIALNRNASILHYTKLENQSPQPRRSFLIDAGANFFGYASDITRTYAFEKNIFSELIEAMDRAQLEIIDTMRPGVKYVDLHLATHQKVAQMLIDFDLATGDREGLIEQGITSVFFPHGLGHMLGLQVHDMGGFLHDERGTHIAAPDAHPFLRCTRTLAANQVLTIEPGLYIIDSLLQGLKQDNRQHQVNWNSVDLLRPFGGIRIEDNVIVHSDKNENMTRDLGLD
|
Splits dipeptides with a prolyl residue in the C-terminal position.
|
A8FP64
|
C3KUS7
|
TSAD_CLOB6
|
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
|
Clostridium
|
MKESINILAIESSCDETSAAVVINGREVLSNIIASQISTHEKFGGVVPEVASRKHIEVISAVVQEALDEANFTLDDIDAIGVTYGPGLVGALLVGLQYAKGLAFATGKPLIGVNHIEGHISANFIEYKDLKPPFMCLVVSGGHTFIVYMKDYGEFEVLGETRDDAAGEAFDKVARAIGLGYPGGPKIDKISKEGNEEAIKFPRANFHDDTLDFSFSGIKSAVLNYLNKKEMKGEEINRADVAASFQKSVVDVLVDNTIKACMSKKVDKIAVAGGVAANSCLRETLVRECKKKGIEVLIPPFILCTDNAAMIGSAAYFEYIKGRRTSLDINAVPNLKLGER
|
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
|
C3KUS7
|
A8FX76
|
ASTB_SHESH
|
N-succinylarginine dihydrolase
|
Shewanella
|
MKHFEANFDGLVGPTHNYAGLSFGNVASLNNAAATSNPRAAAKQGLKKAKALADMGMVQGMLAPQERPDLHTLRRIGFSGTDAEILNKAAKEAPALLRACCSASSMWTANAATVSPSADTHDGKLHFTPANLVDKLHRSIEPETTGNILAATFNNSRHFAHHQHLPEHSSFGDEGAANHTRLCKDYGNAGVELFVYGQEATNPAAPKPSKFPARQTLEASQAIARLHQLDDENTVFISQNPDVIDQGVFHNDVIAVGNQNVLFYHEQAFLDTKRKLDEIKRKFGDSELHFIEVPTSRVAIQDAVKSYLFNTQIITLPSGEMAIIAPTNCQENEAVHAYLNEVVTLGSPIKQVNYFDVKQSMQNGGGPACLRLRVAMNDMELAAVNQHTLMNDALFTRLNAWVDKHYRDRLSVDDLADPQVLIESRTALDELTQIMKLGSVYQFQK
|
Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-succinylornithine, ammonia and CO(2).
|
A8FX76
|
B0VMZ7
|
UNG_ACIBS
|
Uracil-DNA glycosylase
|
Acinetobacter calcoaceticus/baumannii complex
|
MQLTEQQQDKLSKVQLEESWKRSLTSFLLSPYMDSLRDFLFQQKQAQKTIYPPSKQIFNALNITPLDHVKVVILGQDPYHGPNQANGLSFSVQRGVALPPSLRNIFHELHTDLGVPVSRHGDLTKWAEQGVLLLNSVLTVEAGQPTSHHKQGWEEFTDAVIDVLNEQREHIVFILWGAYAQRKGQRINREKHLVLTAAHPSPLAANRGGFFGCKVFSKTNQYLKQHGIEPIDWQLDA
|
Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
|
B0VMZ7
|
Q1QT79
|
ARGB_CHRSD
|
NAG kinase
|
Chromohalobacter
|
MSENARDPRLVVEILSEALPYIQRFSGKTVVVKYGGNAMTEDTLIDSFARDMVLMKEVGINPVVVHGGGPQIGELLERLNIESRFVGGMRVTDAETMDVVEMVLGGLVNKSIVNLINRSGGKAIGLTGKDGAQITARQLRVEHQTPEMTAPEIIDIGHVGEVEHIATDLIEMLAARDFIPVIAPIGVDAEGHSYNINADLVAGKVAEALGAEKLMLLTNVAGLMNAEGEVMTGLSTAQVDAMIGDGTIHGGMLPKIRCALEAVKGGVASSHIIDGRVPHATLLEIFTNAGVGTLITDTASDVSPED
|
Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
|
Q1QT79
|
P9WJV1
|
MMPL5_MYCTU
|
Siderophore exporter MmpL5
|
Mycobacterium tuberculosis complex
|
MIVQRTAAPTGSVPPDRHAARPFIPRMIRTFAVPIILGWLVTIAVLNVTVPQLETVGQIQAVSMSPDAAPSMISMKHIGKVFEEGDSDSAAMIVLEGQRPLGDAAHAFYDQMIGRLQADTTHVQSLQDFWGDPLTATGAQSSDGKAAYVQVKLAGNQGESLANESVEAVKTIVERLAPPPGVKVYVTGSAALVADQQQAGDRSLQVIEAVTFTVIIVMLLLVYRSIITSAIMLTMVVLGLLATRGGVAFLGFHRIIGLSTFATNLLVVLAIAAATDYAIFLIGRYQEARGLGQDRESAYYTMFGGTAHVVLGSGLTIAGATFCLSFTRLPYFQTLGVPLAIGMVIVVAAALTLGPAIIAVTSRFGKLLEPKRMARVRGWRKVGAAIVRWPGPILVGAVALALVGLLTLPGYRTNYNDRNYLPADLPANEGYAAAERHFSQARMNPEVLMVESDHDMRNSADFLVINKIAKAIFAVEGISRVQAITRPDGKPIEHTSIPFLISMQGTSQKLTEKYNQDLTARMLEQVNDIQSNIDQMERMHSLTQQMADVTHEMVIQMTGMVVDVEELRNHIADFDDFFRPIRSYFYWEKHCYDIPVCWSLRSVFDTLDGIDVMTEDINNLLPLMQRLDTLMPQLTAMMPEMIQTMKSMKAQMLSMHSTQEGLQDQMAAMQEDSAAMGEAFDASRNDDSFYLPPEVFDNPDFQRGLEQFLSPDGHAVRFIISHEGDPMSQAGIARIAKIKTAAKEAIKGTPLEGSAIYLGGTAAMFKDLSDGNTYDLMIAGISALCLIFIIMLITTRSVVAAAVIVGTVVLSLGASFGLSVLIWQHILGIELHWLVLAMAVIILLAVGADYNLLLVARLKEEIHAGINTGIIRAMGGSGSVVTAAGLVFAFTMMSFAVSELTVMAQVGTTIGMGLLFDTLIVRSFMTPSIAALLGKWFWWPQVVRQRPIPQPWPSPASARTFALV
|
Overexpression of the system confers non-target based resistance to azoles, clofazimine and bedaquiline, via an efflux mechanism.
|
P9WJV1
|
A4T8K3
|
ATPE_MYCGI
|
F-ATPase epsilon subunit
|
Mycolicibacterium
|
MADLHVEIVAVERELWSGDATFVFTRTTAGEIGILPRHIPLVAQLVDDAMVRVEREGEDDLRIAVDGGFLSVTEEAVRILVENAEFESEINADAAKQDSESDDERTAAWGRARLRALGQLD
|
Produces ATP from ADP in the presence of a proton gradient across the membrane.
|
A4T8K3
|
B7IPS7
|
HPRK_BACC2
|
HPr(Ser) kinase/phosphorylase
|
Bacillus cereus group
|
MPKVRTKDLIEQFQLELISGEEGIHRPIDTSDLSRPGIEMAGFFTYYPADRVQLLGKTELTFFDTLTTEQKQERMKALCTEETPCIIITRNQDVPDELLQASRESGMPLLRSSQTTTRLSSRLTNYLEGKLAPTTAVHGVLVDIYGVGVLITGQSGVGKSETALELVKRGHRLVADDSVEIRQEDEDTLVGSSPDLIEHLLEIRGLGIINVMTLFGAGAVRNYKRITLVINLEIWDQKKNYDRLGLDEEKMKIIDTELTKITLPVRPGRNLAVIIEVAAMNFRLKRMGVNAAQQFSERLMSAIELGNQE
|
Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr). The two antagonistic activities of HprK/P are regulated by several intracellular metabolites, which change their concentration in response to the absence or presence of rapidly metabolisable carbon sources (glucose, fructose, etc.) in the growth medium. Also phosphorylates/dephosphorylates the HPr-like catabolite repression protein crh on a specific serine residue. Therefore, by controlling the phosphorylation state of HPr and crh, HPrK/P is a sensor enzyme that plays a major role in the regulation of carbon metabolism and sugar transport: it mediates carbon catabolite repression (CCR), and regulates PTS-catalyzed carbohydrate uptake and inducer exclusion.
|
B7IPS7
|
P49084
|
GPA1_SOYBN
|
Guanine nucleotide-binding protein alpha-1 subunit
|
Glycine subgen. Soja
|
MGLVCSRSRRFREAHAEENAQDAEIERRIELETKAEKHIQKLLLLGAGESGRSTIFKQIKLLFQTGFNEAELKSYIPVVHANVYQTIKVLQDGSKELAQNDFDSSKYVISNENQDIGQKLSEIGGTLVYPRLTKELAQEIETMWEDAAIQETYARGNELQVPDCAHYFMENLERLSDANYVPTKEDFLYARVRTTGVVEIQFSPVGENKRSGEVYRLFDVGGQRNERRKWIHLFEGVTAVIFCSAISEYDQTLYEDENKNRMMETKELFEWVLRQPCFEKTSFMLFLNKFDIFEKKVLNVPLNVCEWFKHDYQPVSTEKQEIEHAYEFVKKKFEELYFQSTAPDCVDRVFKIYQATAPDQKLVKKTFKLGDETLRRRNPLEAGLL
|
Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.
|
P49084
|
A1TRH1
|
GLYA_ACIAC
|
Serine hydroxymethyltransferase
|
Acidovorax
|
MYQRNILVEQADPEVWAAIQAENLRQEQHIELIASENYASPAVMAAQGSQLTNKYAEGYPGKRYYGGCENVDVVEQLAIDRVKKLFGADAANVQPNSGSQANQAVLLAFLKPGDTILGMSLAEGGHLTHGMPLNMSGKWFNIVSYGLNEKEEIDYDALEAKAREHKPKLIIAGASAYSLRIDFERFAKIAKEVGAIFWVDIAHYAGLVVAGEYPNPVPFADVVTSTTHKSLRGPRGGIILMKAEHEKAINSAIFPGLQGGPLEHVIAAKAVAFKEALTPEFKAYQQQVAKNAKVFAETLIERGLRIISGRTESHVMLVDLRAKGITGKAAEAALGQAHITINKNSIPNDPEKPMVTSGIRVGTPAITTRGFKEEETRITANLLADVLENPNDEANLAAVREKVHALTSRFPVYR
|
Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
|
A1TRH1
|
A4GYP0
|
MATK_POPTR
|
Intron maturase
|
Populus
|
MKIEKSQRNLEIDRSRKNDFLYPLIFREYIYTFAHDRDLNRSILLENVGYDNKYSLLIVKRLITRMYQQNHLIISANDSNQNTFFRYNKNLYFQMISEGFAVIVEIPFSLRLVSSLESSEIVKSHNLRSIHSIFPFLEGKFPHLNYLSEGLIPYPIHLEKLVQILRYWVKDPSSLHLLRLFLHEYWNLNSLIIPKKSISFFVKKNQRFFLFLYNSHVYEYESVFFFLCKQSFHFRLTFYQVFLERIYFYGKIEHFVEVFTKDWGDSLCLLKDPFIHYIRYQGKSIFVSKDTPLLMKKWKYYLVNLCQCHFDVCFQPQKIHINPFSLYKHSFALLGYLSSSSVRLNLSVVRSQMLENAFLMDNIMNKLDTTVSIIPLIGSLAKMKFCNAVGHPISKPTWADFSDSDIIDRFVRICRNLSHYYSGSSRKKSLYRIKYILRLSCVKTLARKHKSTVRIFLKRLGSELLEEFFTEEEQILFLIFPRASSISQKLYRGRVWYLDIICINELSNHE
|
Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns.
|
A4GYP0
|
A2ZET6
|
ARFW_ORYSI
|
OsARF1
|
Oryza sativa
|
MATAEVGGGGGEGDAAAAAVARAGGGGGGGGGGGEDALFTELWSACAGPLVTVPRVGEKVFYFPQGHIEQVEASTNQVGEQRMQLYNLPWKILCEVMNVELKAEPDTDEVYAQLTLLPELKQQEDNGSTEEEVPSAPAAGHVRPRVHSFCKTLTASDTSTHGGFSVLRRHADECLPPLDMSRQPPTQELVAKDLHGVEWRFRHIFRGQPRRHLLQSGWSVFVSAKRLVAGDAFIFLRGENGELRVGVRRAMRQQTNVPSSVISSHSMHLGVLATAWHAVNTGTMFTVYYKPRTSPAEFVVPYDRYMESLKRNYSIGMRFKMRFEGEEAPEQRFTGTIVGMGDSDPAGWPESKWRSLKVRWDEASSIPRPERVSPWQIEPAVSPPPVNPLPVPRTKRLRPNATALPADSSAIAKEAATKVVVESEPNGTQRTFQTQENATPKSGFGNSSELESAQKSIMRPSGFDREKNNTPIQWKLGSDGWMQMSKPESYSEMLSGFQPPKDVQTPQGFCSLPEQITAGHSNFWHTVNAQYQDQQSNHNMFPSSWSFMPPNTRLGLNKQNYSMIQEAGVLSQRPGNTKFGNGVYAALPGRGTEQYSGGWFGHMMPNSHMDDTQPRLIKPKPLVVAHGDVQKAKGASCKLFGIHLDSPAKSEPLKSPSSVVYDGTPQTPGATEWRRPDVTEVEKCSDPSKAMKPLDTPQPDSVPEKPSSQQASRNMSCKSQGVSTRSCKKVHKQGIALGRSVDLTKFNGYEELIAELDDMFDFNGELKGPKKEWMVVYTDNEGDMMLVGDDPWIEFCDMVHKIFIYTREEVQRMNPGTLNSRSEDSHANSMERGSVGREMRGCLSTSSLNSENC
|
Auxin response factors (ARFs) are transcriptional factors that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs).
|
A2ZET6
|
Q5E225
|
MURB_ALIF1
|
UDP-N-acetylmuramate dehydrogenase
|
Aliivibrio
|
MQILLNKTLKPYNSFSVNESADLIIQADSIQDLIDIWSDKKYTDMTKLPLGRGSNTLFCNHFNGVVVLNRLFGKSVTETDTDYLLKISSGEDWPALVEWCVDNGFAGIENLAMIPGCAGSAPIQNIGAYGLELKDICESVEYLDLETLQIKTLKNSECLFGYRESIFKHELKDRCIITAITLRLNKQWQPVLAYGPLSDLRNSKTTPKNVFDKICEIRSKKLPDPNVIGNAGSFFKNPVISEEHYLALCETYPNLPAYDVTEGKKIAAGWLIDNAGLKGFKINGAQVHQEQALVLINTGTATSEDILELANHVKNSVLDMYDIELEHEVRFYLNGEESFLSELFDERTH
|
Cell wall formation.
|
Q5E225
|
O07545
|
YHED_BACSU
|
Endospore coat-associated protein YheD
|
Bacillus
|
MNPKRFLIGIDKTSENTLFLPSSLKQDGLLHAAFGTKVVRCHVAYRRHLEQTVLLSENLFHELLLPHRSRADILIHDHTVHIGPLVGIFTAGFTVSLERPFKDRSLFFSKLVTLHEQAGGYCFVFGAHQINWEEGTIEGLLYRENGWEKKIVPLPNVVYDRLPNRKIEDSLLLQHTKKRLIDEYQIPWFNKTFFNKWNVHQLLEKDPRTAPFLPRSELTPSVELIDELCGAYKKVYIKPANGALGTGIYQLTRTDGGLTVKHTNDAKTFTSIDYSDAASFLAEFQKHHNPSDFLIQQGVDLIEFQGKPADFRVHTNKNRKGKWTVTAIAVKISGKNSITTHLSNGGTVKTLAEVYDDPAERVEVIKKLSAAALTASHVLHDHIEGFIGEIGFDFGIDQNGKVWMFEANSRPGRSIFSHPNLHHVDSLTKRRSFEYASYLSEKAITSPEALWPS
|
Involved in sporulation.
|
O07545
|
P86899
|
CYCM_CLITE
|
Cyclotide cter-M
|
Clitoria
|
MAYVRLTSLAVLFFLAASVMKTEGGLPTCGETCTLGTCYVPDCSCSWPICMKNHIIAANAKTVNEHRLLCTSHEDCFKKGTGNYCASFPDSNIHFGWCFHAESEGYLLKDFMNMSKDDLKMPLESTN
|
Probably participates in a plant defense mechanism. Displays insecticidal activity against H.armigera. Has weak hemolytic activity. Binds to phospholipid membranes.
|
P86899
|
O29844
|
GGGPS_ARCFU
|
Phosphoglycerol geranylgeranyltransferase
|
Archaeoglobus
|
MRWRKWRHITKLDPDRTNTDEIIKAVADSGTDAVMISGTQNVTYEKARTLIEKVSQYGLPIVVEPSDPSNVVYDVDYLFVPTVLNSADGDWITGKHAQWVRMHYENLQKFTEIIESEFIQIEGYIVLNPDSAVARVTKALCNIDKELAASYALVGEKLFNLPIIYIEYSGTYGNPELVAEVKKVLDKARLFYGGGIDSREKAREMLRYADTIIVGNVIYEKGIDAFLETLP
|
Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P). This reaction is the first ether-bond-formation step in the biosynthesis of archaeal membrane lipids. To a much lesser extent, is also able to use heptaprenyl pyrophosphate (HepPP; 35 carbon atoms) as the prenyl donor.
|
O29844
|
P0DB56
|
KUP_STRP3
|
Probable potassium transport system protein kup
|
Streptococcus
|
MSDSHLTAFDKASKAGFIIALGIVYGDIGTSPLYTMQSLVENQGGVNQVSESFILGSISLIIWTLTLITTIKYVLIALKADNHHEGGIFSLFTLVRKMSPWLIVPAMIGGATLLSDGALTPAVTVTSAIEGLKAVPGLSHIYQNQTNVIITTLVILIVLFGIQRFGTGFIGKIFGPVMFIWFSFLGVSGFFNMLGHLEIFKAINPYYALHLLFSPENHRGIFILGSIFLATTGAEALYSDLGHVGRGNIYVSWPFVKMCIVLSYCGQAAWILANKHSGIELNPFFASVPSQLRVYLVSLATLAAIIASQALISGSFTLVSEAMRLKIFPLFRVTYPGANLGQLYIPVINWILFAVTSCTVLAFRTSAHMEAAYGLAITITMLMTTILLKYYLIKKGTRPILAHLVMAFFALVEFIFFLASAIKFMHGGYAVVILALAIVFVMFIWHAGTRIVFKYVKSLNLNDYKEQIKQLRDDVCFDLYQTNVVYLSNRMQDHMIDRSILYSILDKRPKRAQVYWFVNVQVTDEPYTAKYKVDMMGTDYMVRVNLYLGFRMPQTVPRYLRTIVQDLMESGRLPKQEQEYTITPGRDVGDFRFVLIEERVSNARQLSNFERFIMQTKASIKHVTASPMRWFGLQYSEVTLEVVPLILSDILKLPIKELVPVEDSEA
|
Transport of potassium into the cell.
|
P0DB56
|
A3DMQ4
|
RS4_STAMF
|
30S ribosomal protein S4
|
Staphylothermus
|
MGDPKKPRKKWEGPRHPWRKEVLVQELKLLGTYGLRNKRELWRAQTIVRKFRHQARSLLAAPQEIREQAEKALLNRLYRLGLLHENASLEDVLGLTVEDLLERRLQTIVYKKGLARTIYHARQLIIHGHIAIAGRRITSPGYIVSREEEDLVDYAPTSPFKKSIEEKA
|
With S5 and S12 plays an important role in translational accuracy.
|
A3DMQ4
|
B2FNL4
|
NUSB_STRMK
|
Antitermination factor NusB
|
Stenotrophomonas maltophilia group
|
MNKNTQGKPSGKPVRRDGVDPVLRSRARRRAVQAIYAWQISGGNAQSLIAQFAHEQAREIADLAYFEALLHGVLDNRRDIDEALGPYLDRGIEEVDAIERAVLRLAGYELRYRLDVPYRVVINEAIESAKRFGSEHGHTYVNGVLDRAAVEWRKVESGH
|
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.
|
B2FNL4
|
Q8Q0Q0
|
TRM56_METMA
|
tRNA ribose 2'-O-methyltransferase aTrm56
|
Methanosarcina
|
MKRIVLLRLGHRPERDKRITTHVGLTARMLGAEGMLLASDDSGIVQSLEDVVRRWGGNFYIKNNVSFKQEIRNWKEGGGKVCHLSMYGVNLPDLADELKKCDKLMIVVGAEKVPPEIYQLADWNVAVGSQPHSEVAAVAITMDRIAEGEPLEKEFPGAELTIVPAERGKHVIENAGE
|
Specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs.
|
Q8Q0Q0
|
B2IPW6
|
XERS_STRPS
|
Tyrosine recombinase XerS
|
Streptococcus
|
MKREILLERIDKLKQLMPWYVLEYYQSKLAVPYSFTTLYEYLKEYDRFFSWVLESGISNADKISDIPLSVLENMSKKDMESFILYLRERPLLNANTTKQGVSQTTINRTLSALSSLYKYLTEEVENDQGEPYFYRNVMKKVSTKKKKETLAARAENIKQKLFLGDETEGFLTYIDQEHPQQLSNRALSSFNKNKERDLAIIALLLASGVRLSEAVNLDLRDLNLKMMVIDVTRKGGKRDSVNVAAFAKPYLENYLAIRNQRYKTEKTDTALFLTLYRGVPNRIDASSVEKMVAKYSEDFKVRVTPHKLRHTLATRLYDATKSQVLVSHQLGHASTQVTDLYTHIVNDEQKNALDSL
|
Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division.
|
B2IPW6
|
O35867
|
NEB1_RAT
|
p180
|
Rattus
|
MLKAESSGERTTLRSASPHRNAYRTEFQALKSTFDKPKPDGEQKTKEGEGSQQSRGRKYGSNVNRIKNLFMQMGMEPNENAAIIAKTRGKGRPSSPQKRMKPKEFVEKTDGSVVKLESSVSERISRFDTMHDGPSYAKFTETRKMFERSGHESGQNNRHSPKKEKAGEAEPQDEWGGSKSNRGSSDSLDSLSPRTEAVSPTVSQLSAVFENSESPGAITPGKAENSNYSVTGHYPLNLPSVTVTNLDTFGRLKDSNSRPSSNKQATDTEEPEKSEAVPVPEVAQKGTSLASLPSEERQLSTEAEDVTAQPDTPDSTDKDSPGEPSAESQAMPKSNTLSRPKEPLEDAEANVVGSEAEQPQRRDLTGGGDLTSPDASASSCGKEVPEDSNSFEGSHVYMHSDYNVYRVRSRYNSDWGETGTEQDEGDDSDENNYYQPDMEYSEIVGLPQEEEIPANRKIKFSCAPIKVFNTYSNEDYDRRNDDVDPVAASAEYELEKRVEKLELFPVELEKDEDGLGISIIGMGVGADAGLEKLGIFVKTVTEGGAAQRDGRIQVNDQIVEVDGISLVGVTQNFAATVLRNTKGNVRFVIGREKPGQVSEVAQLISQTLEQERRQRELLERHYAQYDADDDETGEYATDEEEDEVGPILPGGDMAIEVFELPENEDMFSPSDLDTSKLSHKFKELQIKHAVTEAEIQKLKTKLQAAENEKVRWELEKNQLQQNIEENKERMVKLESYWIEAQTLCHTVNEHLKETQSQYQALEKKYNKAKKLIKDFQQKELDFIRRQEVERKKLEEVEKAHLVEVQGLQVRIRDLEAEVFRLLKQNGTQVNNNNNIFERRPSPGEVSKGDTMENVEVKQTSCQDGLSQDLNEAVPETERLDSKALKTRAQLSVKNRRQRPTRTRLYDSVSSTDGEDSLERKNFTFNDDFSPSSTSSADLSGLGAEPKTPGLSQSLALSSDESLDMIDDEILDDGQSPKHTQSQSRAVHEWSVQQVSHWLVGLSLDQYVSEFSAQNISGEQLLQLDGNKLKALGMTSSQDRALVKKKLKEMKMSLEKARKAQEKMEKQREKLRRKEQEQMQRKSKKSEKMTSTTEQP
|
Binds to actin filaments (F-actin) and shows cross-linking activity. Binds along the sides of the F-actin. May be involved in neurite formation. Inhibits protein phosphatase 1-alpha activity. May play an important role in linking the actin cytoskeleton to the plasma membrane at the synaptic junction.
|
O35867
|
A8G4T4
|
ARGC_PROM2
|
N-acetyl-glutamate semialdehyde dehydrogenase
|
Prochlorococcus
|
MNVAIVGATGYGGIQAVNLLKKNKNYKISFLGGNKTSGSKWNDNFPFIYLDNDPYVEEISVDNISKNSDVALLCLPNGLSSTLTRKLLERGLKVIDLSADYRYKSLDEWKKVYSKEAAIYKRNDDDLCKEAVYGLPEINKEAISKGRLIACPGCYPTSALIPLAPYLSQGIIENEGIVIDSKSGTSGGGREPNQKLLLSECGEGLSAYGLINHRHTSEIEQVASLISGNKIELLFTPHLVPIPRGMHSTIYGRLRDPGLTSDDCRILLDNYYRNFKNIKVLPVDTFPSTKWVKNTNQIFLSVKVDIRNGRIIILSAIDNLLKGQTGQAIQNLNIMSGFSMDEGLELTNNYP
|
Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
|
A8G4T4
|
Q2SUG3
|
HEM1_BURTA
|
Glutamyl-tRNA reductase
|
pseudomallei group
|
MQLLTIGINHHTAPVALRERVAFPLEQIKPALSTFKSVFLGHPAPNAPEAAILSTCNRTELYCATDDRAARDAAIRWMSDYHRIPADELAPHVYALPQSEAVRHAFRVASGLDSMVLGETQILGQMKNAVRTASEAGSLGTYLNQLFQRTFAVAKEVRGTTEIGAQSVSMAAAAVRLAQRIFEQVAQQRVLFIGAGEMIELCATHFAAQGPRELVVANRTAERGAKLAERFGGRAMPLSDLPARMHEFDIIVSCTASTLPIIGLGAVERAVKARRHRPIFMVDLAVPRDIEPEVGKLKDVFLYTVDDLGAIVREGNASRQAAVAQAEAIIETRVQNFMQWLDARSIVPVIRHMHTQADALRRAELERARKMLARGDDPAAVLDALSQALTNKLIHGPTSALNRANGADRDSLIDLMRGFYQHAPRSSDTSDH
|
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
|
Q2SUG3
|
Q5QZ50
|
AROA_IDILO
|
5-enolpyruvylshikimate-3-phosphate synthase
|
Idiomarina
|
MVNSIHLEPRQHCRGTVTLPGSKSIANRALLMAALCQTPVILHNLLVSDDTSRMREALNALGVSFEDDKLITRVNGLGGGWNKPASELYLGNAGTAMRPLIAVLAATLKNEHQAVVLKGDARMHERPVKHLIDAIQPRGAGVNYLGETGFPPLEMTSGLKPGDFEIDGSVSSQFISALLMALPLLPGDSTLTLKGNVVSRPYIELTLQMLSDFGISIKEDSPQCYAIPGGQCYQSPGEYWVEGDASAASYWMAAALLGKGPVEIIGVGKNSIQGDKRFAEVIEAMGASVSYRKNSMTVSGTGSVQGIDQDFNDIPDAAMTVAPLALFANKPTTIRNVANWRVKETDRLHAMATELRKLGATVDEGEDFLRIEPLKHWRHIAIDTYDDHRMAMCFSLVAFSSAGVTINDPGCCAKTYPDYFSEFSRLCHS
|
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
|
Q5QZ50
|
P25687
|
MIT1_DENPO
|
Black mamba venom protein A
|
Dendroaspis
|
AVITGACERDLQCGKGTCCAVSLWIKSVRVCTPVGTSGEDCHPASHKIPFSGQRMHHTCPCAPNLACVQTSPKKFKCLSKS
|
Potent agonist for both PKR1/PROKR1 and PKR2/PROKR2 . Potently contracts gastrointestinal (GI) smooth muscle .
|
P25687
|
B2ACV0
|
GFA_PODAN
|
S-(hydroxymethyl)glutathione synthase
|
Podospora anserina
|
MVSLHPLLDNGITPGSDSFPGGTLKCLCPSFPVEITLTTNVAHNHACGCSKCWKPAGALFSIVGVVPRDELSVTANGDKLAIVDESAVIQRYACKECGTHLYRRIEKEHPFYGLDFVHAELSEEEGWQEPQFAAFVSSVIEQGFDPAKIGEVRARFRELGLETYDSLSPPLMDAIAAWTGRKNGKYDLHSWLDCERRKGGGGGGQPGGVVCRL
|
Catalyzes the condensation of formaldehyde and glutathione to S-hydroxymethylglutathione.
|
B2ACV0
|
A4SPS7
|
DAPE_AERS4
|
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase
|
Aeromonas
|
MSDVIALAKDLIRRPSVTPQDEGCQTLMSERLARLGFVIEPMVFEDTTNLWARRGSEGPLFCFAGHTDVVPAGPLEKWHTPPFEPTIQDGVLYGRGAADMKGSLAAMVVAVERFVAEHPDHKGSIAFLITSDEEGPFINGTVRVIDTLEARNEKIRWCIVGEPSSTHVVGDVVKNGRRGSITGDLLVRGVQGHVAYPHLADNPIHKAAPALTELAATVWDEGNAYFPPTSFQIANIQAGTGASNVIPGELQVQFNFRFSTQLTDMDIRERVQALLDKHGLDYELTWTLSGQPFLTDTGALLEATVAAVAAVNGQQPALLTTGGTSDGRFIAPTGAEVIELGPVNATIHKVNECVKAEDLDLLAEMYQGVLERLLA
|
Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls.
|
A4SPS7
|
P35738
|
ODBB_RAT
|
Branched-chain alpha-keto acid dehydrogenase E1 component beta chain
|
Rattus
|
MAAVAARAGGLLRLGAAGAERRRRGLRCAALVQGFLQPAVDDASQKRRVAHFTFQPDPESLQYGQTQKMNLFQSITSALDNSLAKDPTAVIFGEDVAFGGVFRCTVGLRDKYGKDRVFNTPLCEQGIVGFGIGIAVTGATAIAEIQFADYIFPAFDQIVNEAAKYRYRSGDLFNCGSLTIRAPWGCVGHGALYHSQSPEAFFAHCPGIKVVIPRSPFQAKGLLLSCIEDKNPCIFFEPKILYRAAVEQVPVEPYKIPLSQAEVIQEGSDVTLVAWGTQVHVIREVASMAQEKLGVSCEVIDLRTIVPWDVDTVCKSVIKTGRLLISHEAPLTGGFASEISSTVQEECFLNLEAPISRVCGYDTPFPHIFEPFYIPDKWKCYDALRKMINY
|
The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
|
P35738
|
A9KVC7
|
PCKA_SHEB9
|
Phosphoenolpyruvate carboxykinase (ATP)
|
Shewanella
|
MADGLNRVHFNPSTAQLVEFALLRGEGELTANGALVAKTGARSGRSPGDRFIVREPSSEAEIEWGPVNQAFDPGAFEGLWARVEAYLADKELFVSDLEVGADTEHYQPVRVTTQYAWHQLFARNLFIIPEEFNRKDKPVWQIINAPDFVCDPERDGTNSDATVILNFAERKVLLAGLKYAGEMKKSMFSVQNFLLPAQGVLPMHCSANVGKDGDTTLFFGLSGTGKTTLSADPKRFLIGDDEHGWAPGGVFNIEGGCYAKCIDLSQKNEPVIWDAIRFGTVLENVVMDEHRVPNYKDSSLTENTRAAYPLEHIAQRKEDNCGAEPHAVVFLTCDVSGVLPPVSILTKEQAAYHFLSGYTAKVGSTEIGSTSAIQSTFSTCFGAPFFPRPAGVYAELLMKRIESFGSQVYLVNTGWTGGPHGVGKRFDIPTTRAIVDAIVSGELKDVETVHLDTLNLAVPVAVSGVDSNLLNPINTWGDKALYAEYAQKLAEAFTKNFAKYQVSDAIRNAGPKA
|
Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
|
A9KVC7
|
Q8GSM7
|
HST_TOBAC
|
Hydroxycinnamoyl-Coenzyme A shikimate/quinate hydroxycinnamoyltransferase
|
Nicotiana
|
MKIEVKESTMVKPAAETPQQRLWNSNVDLVVPNFHTPSVYFYRPTGSPNFFDGKVLKEALSKALVPFYPMAGRLCRDEDGRIEIDCKGQGVLFVEAESDGVVDDFGDFAPTLELRQLIPAVDYSQGIQSYALLVLQITHFKCGGVSLGVGMQHHAADGASGLHFINTWSDMARGLDLTIPPFIDRTLLRARDPPQPQFPHVEYQPPPTLKVTPENTPISEAVPETSVSIFKLTRDQINTLKAKSKEDGNTVNYSSYEMLAGHVWRSTCMARGLAHDQETKLYIATDGRSRLRPSLPPGYFGNVIFTTTPIAVAGDIQSKPIWYAASKLHDALARMDNDYLRSALDYLELQPDLKALVRGAHTFKCPNLGITSWSRLPIHDADFGWGRPIFMGPGGIAYEGLSFILPSPTNDGSQSVAISLQAEHMKLFEKFLYDF
|
Acyltransferase involved in the biosynthesis of lignin. The affinity for shikimate as acceptor is 100-fold higher than for quinate. The most efficient donors are caffeoyl-CoA > p-coumaroyl-CoA > feruloyl-CoA >> sinapoyl-CoA.
|
Q8GSM7
|
A7M958
|
RPOB_CUSRE
|
Plastid-encoded RNA polymerase subunit beta
|
Cuscuta subgen. Monogynella
|
MLVDGKGGITTIPGLNQIQLEGFCRFIDQGLMEELSKFQKIEDIDQEIEFQLFVETYQLVEPLIKERDAVYDSLTYSSELYVSAGLIRKASKDMQEQTIFIGSLPIMNSLGTFIVNGIYRIVINQILQSPGIYYRSELDQNGISVYTGTIISDWGGRLELEIDRKARVWARVSRKQKISILVLLSAMGLNLREILENVCYPEILLSFLRDKEKKKIGSKENAILEFYKKFACVGGDPLFSESLCKELQNKFFQQRCELGRIGRRNMNRRLHLDIPHNNTFLLPRDILEATDHLIGLKFGMGTLDDMNHLQNKRIRSVADLLQDQFGLALVRLENAVQGTLCGAIRHKRIPTPQNLVTSTLLTTTYESFFGLHPLSQVLDGTNPLTQIVHARKVSSLGPGGLTGRTASFRIRDIHPSHYGRICPIDTSEGINVGLIGSLAIHVRIGNWGSLESPFYEISDRLTGVRVLHLSPGRDEYYMVAAGNSLALNQDIQEDQVVPARYRQEFLTIAWEQVNLRSIFPFQYFSIGASLIPFIEHNDANRALMSSNMQRQAVPLTWSEKCIVGTGMERQAALDSGSLAIAEREGRVIYTDTEKILVSGDGKTINIPLVMYQRSNKNTCMYQQPQVRRGQFIKKGQILAGGAATVEGELALGKSVLVAYMPWEGYNFEDAVLISECLVYEDIFTSFHIKKYEIQIHMTTQGPEKVTNEIPHLEAHLIRNLDKNGIVLQGSWVEPGDVLVGKLTPQVVKESAYAPEDRLLRAILGIPVSASKETCLKVPIGARGRVIDVRWIQKKGGYGYNPEKIRVYILQKREIKVGDKVAGRHGNKGIISKILPRQDMPYLQDGRSVDLVFNPLGVPSRMNVGQIFECSLGLAGSLLDRHYRIAPFDERYEQEASRKIVFSELYEASKQTANPWAFEPEYPGKSRIFDGRTGKTFEHPVLIGKPYILKLIHQVDDKIHGRSIGHYALVTQQPLRGRAKQGGQRVGEMEVWALEGFGVAHILQEMLTYKSDHIRARQEVLGTTIVGGTIPSPKNAPESFRLLVRELRSLALELTHFLVSEKNFQVNRKEA
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
A7M958
|
P56829
|
IFNT2_SHEEP
|
Trophoblastin
|
Ovis
|
MAFVLSLLMALVLVSYGPGGSLGCYLSQRLMLDARENLKLLDRMNRLSPHSCLQDRKDFGLPQEMVEGDQLQKDQAFPVLYEMLQQSFNLFYTEHSSAAWDTTLLEQLCTGLQQQLDHLDTCRGQVMGEEDSELGNMDPIVTVKKYFQGIYDYLQEKGYSDCAWEIVRVEMMRALTVSTTLQKRLTKMGGDLNSP
|
Paracrine hormone primarily responsible for maternal recognition of pregnancy. Interacts with endometrial receptors, probably type I interferon receptors, and blocks estrogen receptor expression, preventing the estrogen-induced increase in oxytocin receptor expression in the endometrium. This results in the suppression of the pulsatile endometrial release of the luteolytic hormone prostaglandin F2-alpha, hindering the regression of the corpus luteum (luteolysis) and therefore a return to ovarian cyclicity. This, and a possible direct effect of IFN-tau on prostaglandin synthesis, leads in turn to continued ovarian progesterone secretion, which stimulates the secretion by the endometrium of the nutrients required for the growth of the conceptus. In summary, displays particularly high antiviral and antiproliferative potency concurrently with particular weak cytotoxicity, high antiluteolytic activity and immunomodulatory properties. In contrast with other IFNs, IFN-tau is not virally inducible.
|
P56829
|
Q87JL4
|
PHNW_VIBPA
|
AEP transaminase
|
Vibrio
|
MKNEYLLLTPGPLSTSETVREAMLKDWCTWDDEYNKDIVEVIRTKLVKLATKHSGYTSVLMQGCGTASVEATIGSAIGKEGKLLVVDNGAYGARIAQIADYLNIPCHVVSPGETSQPHLNEVETALASDPAITHVAIVHCETTTGMLNPIEAFASAAKAHGKVVILDAMSSFGGIPMDIADLGIDFMISSANKCIQGVPGFGFVIAKQTELEKCQDQARSLSLDLYDQWHCMEVNHGKWRFTSPTHTVRAFYQALLELEQEGGIEARHNRYQTNQKTLVAGMRSLGFEPLLSDDLHSPIITSFYSPTHSDYQFKAFYTRLKEQGFVIYPGKVSNADCFRIGNIGEVYPADIERLIGAIEKAMYWQVA
|
Involved in phosphonate degradation.
|
Q87JL4
|
Q3JBZ6
|
IHFA_NITOC
|
Integration host factor subunit alpha
|
Nitrosococcus
|
MALTKADMTETLYQELGLNKREAKEIVEMFFEDIRCALEQGEAVKLSGFGNFELRDKGERPGRNPKTGEEIPITARRVVTFRPGQKLKARVEAYAGGKQ
|
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.
|
Q3JBZ6
|
A1AUV8
|
PANB_PELPD
|
Ketopantoate hydroxymethyltransferase
|
Pelobacter
|
MSDMRKKVTIPDILKMKQERRRITMMTAYDYPFARLVDSGGVDAILVGDSLGVVFSGHDNTLSVTMDEMIYHTRAVARAKPQAVLVTDMPFMSYQVSVEEACRNCGRMIQEGGAQAVKIEGGMNMSHVIRAVTSIDIPVMGHIGLTPQSIHRMGGYRVQGRKEQAERIMEDALAVQAAGAFSIVLEGIPSSLAASITAELSIPTIGIGAGPDCDGQVLVIHDILGLCEKYSPKFVKRYAELAPVITDAVNRYVEEVRSGAFPTEEHSFN
|
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
|
A1AUV8
|
Q92H35
|
RNPA_RICCN
|
Protein C5
|
spotted fever group
|
MSITSLKNQKEFELINKLGKKLHERYFILVIATKLPKIFLESKYNTFLGIKVSRKLNKKAVVRNKIKRRIRHLIRIIVSDSSFKAIKFAMIIIPRKGFEEINFSHLNYELSKVILRNI
|
RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
|
Q92H35
|
A7HWT5
|
RPOA_PARL1
|
Transcriptase subunit alpha
|
Parvibaculum
|
MIQKNWEELIKPNKLEINPGHDAQRFATVVAEPLERGFGLTLGNALRRVLMSSLQGAAVTAVQIDGVLHEFSSIAGVREDVTDIILNIKQLALRLHAEGPKRMSLSKKGPGVVTAGDITAGADIEVLNPDLVLCTLDEGAEIRMEFTVALGKGYVASDRNRPEDAPIGLMPVDSLYSPVKRVSYKVENTREGQVLDYDKLTLQIETNGAITPDDAVAYAARILQDQLQTFVNFEEPEQKHVEESRPELEFNAALLKKVDELELSVRSANCLKNDNIVYIGDLIQKTESEMLRTPNFGRKSLNEIKEVLAQMGLHLGMEVPNWPPENIEELAKRYEDQY
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
A7HWT5
|
Q9KSS7
|
RLUB_VIBCH
|
rRNA-uridine isomerase B
|
Vibrio
|
MSEKLQKVLARAGHGSRRELEALIRAGRVSVNGKVAVLGERLEDDNAVVRIDGHVVSVKAQEEVICRVLAYYKPEGELCTRHDPEGRRTVFDRLPKIRGSRWISVGRLDANTSGLLLFTTDGELANRLMHPSRQVEREYLVRVFGDVTEEKVRNLVRGVQLEDGMARFEDVMYAGGEGINHTFYVVINEGRNREVRRLWESQGTTVSRLKRVRYGDIFLDKKLPRGGWMELDLKQVNYLRELVELRPEKETVLNMAPDAATRKRERTRSQKIRRAVRRHEERISATPGRSGKAPARRKPGGESSTRNKVANQQQSSRKPRG
|
Responsible for synthesis of pseudouridine from uracil-2605 in 23S ribosomal RNA.
|
Q9KSS7
|
Q73GD6
|
RL19_WOLPM
|
50S ribosomal protein L19
|
unclassified Wolbachia
|
MTNLLKKFNEQQMQVLAKEIPEFRPGDDLKVTFKVVDGTSERIQIFEGVCISKRNRGLHSSFAVRKVSHGESIVSQFFVYSPALVSVQVTRKGKVRRAKLYYLCKLFGKAARIKERTTYVKKKSK
|
This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
|
Q73GD6
|
A8EZK0
|
RL18_RICCK
|
50S ribosomal protein L18
|
belli group
|
MRSAKLKFEKRRSRIRHKISQTSNRVRLSIFKSCRHIYAQIIDDSKSITIASASTLDAKIKKLKKSHCNIENAIKVGKAIATKADSAGIKEVVFDRGGYKYHGVVKALADAAREKIKF
|
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.
|
A8EZK0
|
B7JWJ7
|
RSMA_RIPO1
|
S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase
|
Rippkaea orientalis
|
MPQPRKRFAQHWLRSETALDQIIEAAQLNMSDLVLEIGPGTGILTRRLLPLVQSIVAVELDRDLCYRLAKSFGNFNHFLLLEGDILSLDLTTQLEQFPQFQPINKVVANIPYNITSPILEKLLGSIAHPQHPSYELIVLLMQKEVAQRIVASPQSKAYGALSVRTQYLAQCDYICEVPSKAFDPPPKVDSAVIRLTPRSLETPAINPQKLDQLVKLGFANRRKMLHNNLKSIIDKDHLTLLLDQLQINPQVRAEELSLEQWIMFSNLLETVS
|
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.
|
B7JWJ7
|
Q944A7
|
BSK1_ARATH
|
Brassinosteroid-signaling kinase 1
|
Arabidopsis
|
MGCCQSLFSGDNPLGKDGVQPQPLSQNNHGGATTADNGGSGGASGVGGGGGGGGIPSFSEFSFADLKAATNNFSSDNIVSESGEKAPNLVYKGRLQNRRWIAVKKFTKMAWPEPKQFAEEAWGVGKLRHNRLANLIGYCCDGDERLLVAEFMPNDTLAKHLFHWENQTIEWAMRLRVGYYIAEALDYCSTEGRPLYHDLNAYRVLFDEDGDPRLSCFGLMKNSRDGKSYSTNLAYTPPEYLRNGRVTPESVTYSFGTVLLDLLSGKHIPPSHALDMIRGKNIILLMDSHLEGKFSTEEATVVVELASQCLQYEPRERPNTKDLVATLAPLQTKSDVPSYVMLGIKKQEEAPSTPQRPLSPLGEACSRMDLTAIHQILVMTHYRDDEGTNELSFQEWTQQMKDMLDARKRGDQSFREKDFKTAIDCYSQFIDVGTMVSPTVFGRRSLCYLLCDQPDAALRDAMQAQCVYPDWPTAFYMQSVALAKLNMNTDAADMLNEAAQLEEKRQRGGRGS
|
Serine/threonine kinase that acts as positive regulator of brassinosteroid (BR) signaling downstream of the receptor kinase BRI1. Mediates signal transduction from BRI1 by functioning as substrate of BRI1 . Functions as a positive regulator of plant immunity. May be involved in the regulation of pattern-triggered immunity (PTI) downstream of the flagellin receptor FLS2. Possesses kinase activity in vitro. Kinase activity is required for its function in innate immunity .
|
Q944A7
|
Q9XZT6
|
DNK_DROME
|
Multispecific deoxynucleoside kinase
|
Sophophora
|
MAEAASCARKGTKYAEGTQPFTVLIEGNIGSGKTTYLNHFEKYKNDICLLTEPVEKWRNVNGVNLLELMYKDPKKWAMPFQSYVTLTMLQSHTAPTNKKLKIMERSIFSARYCFVENMRRNGSLEQGMYNTLEEWYKFIEESIHVQADLIIYLRTSPEVAYERIRQRARSEESCVPLKYLQELHELHEDWLIHQRRPQSCKVLVLDADLNLENIGTEYQRSESSIFDAISSNQQPSPVLVSPSKRQRVAR
|
Deoxyribonucleoside kinase that has a broad specificity phosphorylating thymidine, 2'-deoxyriboadenosine, 2'-deoxyribocytidine and 2'-deoxyriboguanosine. Specificity is higher for pyrimidine nucleosides. Several anti-viral and anti-cancer nucleoside analogs are also efficiently phosphorylated.
|
Q9XZT6
|
A1RRE2
|
SYM_PYRIL
|
Methionyl-tRNA synthetase
|
Pyrobaculum
|
MAKYVIGSAWPYVQTVPHLGNLIGSVLSADVYARYLRFRGHDVVFVSGSDMHGTPIEVEAIQLGVDPEEYAKKMHQIVAELFKRWDISFDLYTHTHSDTHIKFVQNFFLKIYNNGYIFTKEEEVPYCPRDKIYLPDRFIIGKCPYCGYERARGDQCENCGRLLDPKQLIEPRCAICGSRPEWRITKHWYLDLRKLEDRIRKYVEENPHLPPNAKEMSLGMLKEGLKPRAITRDNKWGIPAPFPGAEGKTIYVWFEAVLGYISAVVELFREDAGKWERYWKDPETKIVFFVGKDNIPFHVIILPALLLANGEGYTLPTTTASTEYLLYEGDKFSKSRRWGIWIDEALQLMPPDYWRFILIYIRPENRDTSFTWALALEIINKIMNDDVGNYINRVLTFIKNRMGGVVPPPGAPTREDEEFINRVIQLFKKAEKHYDAIELKDALHTVVEIAREGNRYLNARAPWELLRRDIEVANAVMYRAYWSLKTIAAGLTPVTPRSAAELWKMLGISQPSWDEAYKPPTPGTPLGDVRPLFRKFTEEEVKDMLKKLEELRSQRASKKYPWEQVLL
|
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
|
A1RRE2
|
Q74D60
|
ISPG_GEOSL
|
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase
|
Geobacter
|
MKAKTRQIRVGNVPVGGDAPCSVQSMCNTDTRDAGATLDQINALAAAGCEIVRCAVPDMAAAEALGAIKRQSPIPVIADIHFDYKLALKVLEGGIDGLRLNPGNIGERWKVEEVVAAARERLVPIRIGVNAGSLEKELLQKYGHPTAEAMVESALGHVRILEELGYDQIKISLKASDVPKTVAAYRLLAQRIDYPLHIGITEAGTMFSGTIKSAVGLGILLADGIGDTLRVSLTGDPVDEVRVGFEILKALNLRQKGINLVSCPTCGRCQINLIGVAEEVEKRLAGIDAHLTVAVMGCVVNGPGEAREADVGIAGGRGEGLLFRNGEIVRKVPEADMADALIAEVEKILAEKH
|
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
|
Q74D60
|
Q97ZE3
|
CREN7_SACS2
|
Chromatin protein Cren7
|
Saccharolobus
|
MSSGKKPVKVKTPAGKEAELVPEKVWALAPKGRKGVKIGLFKDPETGKYFRHKLPDDYPI
|
A highly abundant probable chromatin protein, it binds double-strand DNA without sequence specificity; there is approximately 1 Cren7 molecule for 12 bp of DNA. Constrains negative DNA supercoils, increases DNA stability against thermal denaturation. Binding does not require protein methylation. Binds single-strand DNA weakly.
|
Q97ZE3
|
P57359
|
RIBA_BUCAI
|
GTP cyclohydrolase II
|
Buchnera
|
MQLIEKAMLPTPWGNFLIFGFEEKKNGKNHVALVYGDIKTNTPTLSRVHSECLTGDAFFSLRCDCGSQLEMSMKRISQEGSGVLIYHRQEGRNIGLLNKIKAYALQDRGLDTVQANQKLGFSADERDFSLCADIFNILNIKKIRLLTNNPFKVQMLSDAGINIVERVPLIVKKNPKNAYYLKTKAEKMGHLLSE
|
Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
|
P57359
|
C4LBS7
|
RRAA_TOLAT
|
Regulator of ribonuclease activity A
|
Tolumonas
|
MEYNTSQLCDIYQDQVDVVEPMFSTFGGRSSFGGLVTTIKCFEANGIIRQIVKESGVGRVLLIDGGGSLRRALIDADIAAIAADNGWEGIICYGSVREVDALADLEIGIQALASIPVGADEDDTGDSELPVNFGGVTFLPEDHIYADTTGVILSPEPLDIE
|
Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome. Modulates RNA-binding and helicase activities of the degradosome.
|
C4LBS7
|
A5VJ28
|
RSMH_LIMRD
|
rRNA (cytosine-N(4)-)-methyltransferase RsmH
|
Limosilactobacillus
|
MAEFKHVTVLLKEAVAGLNVQPTGTYVDATLGGGGHTQAILQQLVDGHLYSFDQDQTAIDYNKEHLKTAIEQQKLTLVEDNFRNLKAELNSYNVKHVNGILYDLGVSSPQFDDAKRGFSYQHDAPLDMRMNQEQKLSAMEVVNEWPYERLVKILYRYGEEKFAKSIARKIEQRRKVAPIKTTFELVDVIKEGIPAAARRHGGHPAKKSFQAIRIAVNDELGALEESLEQALDLLDVGGRISVITFQSLEDRLVKTMFREKTSLSGDVPQGLPVIPAGMEPNFKLINKKPIVASDEELAANHRAHSAKLRIIEKIREGK
|
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
|
A5VJ28
|
Q2GG13
|
MUTS_EHRCR
|
DNA mismatch repair protein MutS
|
Ehrlichia
|
MNHDSKITPIMQQYMMLKSQYKEYLLFYRLGDFYELFFDDAIETSRILNIVLTKKGNVPMCGVPFHSSESYLNRLVKLGYKIAICEQLETSEEAKKRGYKALVKRDVVRIVTPGTILEDSLLEAKENNYLSCIVNVDHNYAIAWLELSTGLFYYHTTELHKLDSDLFRINPKEVLISDKLVELDSIYSILRKYKFSVTQYSGSFFDVSRSYNTLCNVYGISTLKGLGDLKNEEIAVCGSLLEYVKATQKGNLPQLEFPKAYSKGDFMFIDAAALRNLELFCTQSGDLEGSLISSIDYTITACGGRLLKRCLSAPLACSHAINRRLDIVEFFVNDRTLCRGVRETLRGIADIERILTRIKVGKCSPKDLYALKLTLDKIFVLLDLLHKFDSSVVGDFCSRLGKYDDLCKTLDDVLIPNNVNNVKDGGFINPDYDAQLSEYIYIQSYSNDLIQELRDKYRNITNIQSLKILYNNILGYYVEVSSSYLISDKDFIHRQTLANSIRYTTSELKALESKIISARDAAINLEVKIFGQLCTCIIEVADKITMTAHAIAEIDMLTSFAELAIQYSYTKPIVDDSYEFNIKKGRHPVVERNGKFVANDIDLSLMQRVHLITGPNMAGKSTFLRQNALIGILAHIGSFVPAQHAHIGVIDKVFSRVGASDNIASGHSTFMVEMTETAAIINQATDKSFVILDEIGRGTGTYDGLSIAWSVIEQIHNVNKSRAIFATHYHELSKLDRYLENIKCFCMKVEEWNGKVVFLHEIIPGSTNKSYGIHVAKLAGFPQSVLDRAEDLMSKLKANEDLLT
|
This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity.
|
Q2GG13
|
Q7W2I1
|
MNMG_BORPA
|
Glucose-inhibited division protein A
| null |
MDFPREFDVIVVGGGHAGTEAALAAARAGAQTLLLTHNIETLGQMSCNPSIGGIGKGHLVKEVDALGGAMAIATDEAGIQFRILNSSKGPAVRATRVQADRVLYRNAMRARLENQPNLWLFQQAVDDLMVQGDQVVGAVTQIGLRFRARTVVLTAGTFLNGLIHVGLQNYSGGRAGDPPANSLGQRLKELQLPQGRLKTGTPPRIDGRSINYSVLEEQPGDLDPVPVFSFLGKASMHPRQLPCWITHTNARTHEIIRGGLDRSPMYSGVIEGVGPRYCPSIEDKIHRFADKASHQVFLEPEGLNTHEIYPNGVSTSLPFDVQYELIHSLPGLENAHILRPGYAIEYDYFDPRALKSTLETKAISGLFFAGQINGTTGYEEAAAQGLLAGANAALQAQGKEPWVPRRDEAYLGVLVDDLVTRGVTEPYRMFTSRAEYRLSLREDNADLRLTEIGRRLGLVDDVRWDAFSRKRDAVAQEVERLKSTWVNPRVLPAHAAEALLGKAIEREYSLSDLLKRPNVSYEALMQARTDEGELLAGPGVLEDDVLAEQVETQVKYAGYIARQQDEVQKHLSHEQQPIPADIDYDAVTSLSFEVRQKLKTHRPETIGQAARVSGVTPAAISLLLIHLKRLHYGSRKQAA
|
NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
|
Q7W2I1
|
P01040
|
CYTA_HUMAN
|
Cystatin-A, N-terminally processed
|
Homo
|
MIPGGLSEAKPATPEIQEIVDKVKPQLEEKTNETYGKLEAVQYKTQVVAGTNYYIKVRAGDNKYMHLKVFKSLPGQNEDLVLTGYQVDKNKDDELTGF
|
This is an intracellular thiol proteinase inhibitor. Has an important role in desmosome-mediated cell-cell adhesion in the lower levels of the epidermis.
|
P01040
|
Q2FHM9
|
KGUA_STAA3
|
GMP kinase
|
Staphylococcus
|
MDNEKGLLIVLSGPSGVGKGTVRKRIFEDPSTSYKYSISMTTRQMREGEVDGVDYFFKTRDAFEALIKDDQFIEYAEYVGNYYGTPVQYVKDTMDEGHDVFLEIEVEGAKQVRKKFPDALFIFLAPPSLEHLRERLVGRGTESDEKIQSRINEARKEVEMMNLYDYVVVNDEVELAKNRIQCIVEAEHLKRERVEAKYRKMILEAKK
|
Essential for recycling GMP and indirectly, cGMP.
|
Q2FHM9
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.