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