Datasets:
habdine
/
Prot2Text-Data

Dataset card Data Studio Files
xet
Community
1
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
Q0SND6
LUXS_BORAP
Autoinducer-2 production protein LuxS
Borreliella
MKKITSFTIDHTKLNPGIYVSRKDTFENVIFTTIDIRIKAPNIEPIIENAAIHTIEHIGATLLRNNEVWAEKIVYFGPMGCRTGFYLIIFGNYESKDLIDLISWLFSEIVNFSEPIPGASHKECGNYKEHNLDMAKYESSKYLQILNNIKEENLKYP
Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD).
Q0SND6
Q3E991
PRK6_ARATH
Pollen receptor-like kinase 6
Arabidopsis
MAAAVLNPGFFLLILLLSFSISPSLQYVSESEPLVRFKNSVKITKGDLNSWREGTDPCSGKWFGIYCQKGLTVSGIHVTRLGLSGTITVDDLKDLPNLKTIRLDNNLLSGPLPHFFKLRGLKSLMLSNNSFSGEIRDDFFKDMSKLKRLFLDHNKFEGSIPSSITQLPQLEELHMQSNNLTGEIPPEFGSMKNLKVLDLSTNSLDGIVPQSIADKKNLAVNLTENEYLCGPVVDVGCENIELNDPQEGQPPSKPSSSVPETSNKAAINAIMVSISLLLLFFIIVGVIKRRNKKKNPDFRMLANNRENDVVEVRISESSSTTAKRSTDSSRKRGGHSDDGSTKKGVSNIGKGGNGGGGGALGGGMGDIIMVNTDKGSFGLPDLMKAAAEVLGNGSLGSAYKAVMTTGLSVVVKRIRDMNQLAREPFDVEMRRFGKLRHPNILTPLAYHYRREEKLVVSEYMPKSSLLYVLHGDRGIYHSELTWATRLKIIQGVAHGMKFLHEEFASYDLPHGNLKSSNVLLSETYEPLISDYAFLPLLQPSNASQALFAFKTPEFAQTQQVSHKSDVYCLGIIILEILTGKFPSQYLNNGKGGTDIVQWVQSSVAEQKEEELIDPEIVNNTESMRQMVELLRVGAACIASNPDERLDMREAVRRIEQVKT
Key receptor for sensing species-specific attractants in cooperation with other pollen receptor-like kinases . Essential for pollen tube reorientation toward attractant peptides .
Q3E991
P42145
HSP1_PSECU
Sperm protamine P1
Pseudochirops
MARYRHSRSRSRSRYRRRRRRRRSRYRGRRRRYRRSRRRRRRGRRRGNCLGRRGYRRRRYSRRRRRRYY
Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex.
P42145
Q2H608
S2538_CHAGB
Solute carrier family 25 member 38 homolog
Chaetomium
MSDGSRTALSKSTFHFAAGLGSGVLSAVLLQPIDLLKTRVQQSGAHSLSAAIADIRAAPRLLPALWRGAVPSALRTGFGSAIYFTSLNAIRQSAARISPLPSSSSSTTTSSSTTTSSSSSSLPKLSNTSNLLAGAAARSLAGLILMPLTVLKVRYESTLYNYTSLASAARDIAAHEGARGFFAGYGATAVRDAPYAGLYVLFYEQGKKRLSQLFPTTTTTTTTNSTQNGPMGLQHAASINFASGVLAGVICSVVSNPFDAVKTRIQLQPGRYRNMVSGARRMVGEEGVRALWDGLALRMSRKAVSSALAWTVYEELIRRAEAGWRAGAARERL
Mitochondrial glycine transporter that imports glycine into the mitochondrial matrix. Plays an important role in providing glycine for the first enzymatic step in heme biosynthesis, the condensation of glycine with succinyl-CoA to produce 5-aminolevulinate (ALA) in the mitochondrial matrix.
Q2H608
Q2SCL1
RUVC_HAHCH
Holliday junction resolvase RuvC
Hahella
MLKVLGIDPGSRFTGYGVVEWGGGKPRYVASGCIRVTGETLAERLRCIYLGVTQVVSMYAPDEAAIEQVFMARNADSALKLGQARGVAILAMAEQGLQVAEYSAKKVKQSVVGKGNAEKWQVQHMMQAMLDLQAKPQADAADALAIAVCHLHTQQSLMRIGSVSSSRRGRMR
Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group.
Q2SCL1
Q16186
ADRM1_HUMAN
Rpn13 homolog
Homo
MTTSGALFPSLVPGSRGASNKYLVEFRAGKMSLKGTTVTPDKRKGLVYIQQTDDSLIHFCWKDRTSGNVEDDLIIFPDDCEFKRVPQCPSGRVYVLKFKAGSKRLFFWMQEPKTDQDEEHCRKVNEYLNNPPMPGALGASGSSGHELSALGGEGGLQSLLGNMSHSQLMQLIGPAGLGGLGGLGALTGPGLASLLGSSGPPGSSSSSSSRSQSAAVTPSSTTSSTRATPAPSAPAAASATSPSPAPSSGNGASTAASPTQPIQLSDLQSILATMNVPAGPAGGQQVDLASVLTPEIMAPILANADVQERLLPYLPSGESLPQTADEIQNTLTSPQFQQALGMFSAALASGQLGPLMCQFGLPAEAVEAANKGDVEAFAKAMQNNAKPEQKEGDTKDKKDEEEDMSLD
Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins . This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required . Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair . Within the complex, functions as a proteasomal ubiquitin receptor . Engages and activates 19S-associated deubiquitinases UCHL5 and PSMD14 during protein degradation . UCHL5 reversibly associate with the 19S regulatory particle whereas PSMD14 is an intrinsic subunit of the proteasome lid subcomplex .
Q16186
Q8W257
PFI_PTIFI
Polyenoic fatty acid isomerase
Ptilota
MSLNRVLHIFLIAYLACTALTHDFDDTIAVVGAGYSGLSAAFTLVKKGYTNVEIYESQGEVGGYVYSVDYNNVAHDLATYALTPAYWKFQEAMKSIGVGFCELDVAIVQTNSTPVSVPFEKWMAAYWAAKVPNPLNLVRKVSTQVSTYVEVWKKLFNMDFIDTSTKRTNRLFPLKTNDVDVLAQFSMPMKDFVALHKLDLLEPLFIQATDSQAYGPYDTTPALYYMVWFPPNLFNGEENTVPCGTYNSMQSMAEHMAEWLKSKGVTFHMNTKVTKISRATDGSSPSLLEEGVATPKLFDTIISTNKLPSANRAEVVTPLLPKEREAADTYEELQMFSALLETNRSDAIPTTGFLMVDADAIIAHDPNTGFWGCLNAERRGGYSDENAILSSDTVTRVSAIYYYTERANNERIDFSLDEKIQQVKTNLATWDSATWTNLTSRTFGGYFQRWRTPDVMGQKPWNLADIQGEGDVYYVNSAACGFESVGHVFDCADNLIKDFF
Involved in the biosynthesis of conjugated triene-containing fatty acids. Catalyzes the isomerization of a wide range of substrates containing three or more methylene interrupted olefins into a Z,E,E conjugated triene functionality. May be involved in a stress tolerance mechanism as response to intertidal habitats with direct sunlight, desiccation and high temperature. In vitro substrates include arachidonic acid ((5Z,8Z,11Z,14Z)-eicosatetraenoic acid), EPA ((5Z,8Z, 11Z,14Z,17Z)-eicosapentaenoic acid), DHA ((4Z,7Z,10Z,13Z,16Z,19Z)-docosahexenoic acid), adrenic acid ((7Z,10Z,13Z,16Z)-docosatetraenoic acid), anandamide (arachidonyl-N-ethanolamide) and eicosatrienoic acid ((5Z,8Z,11Z)-eicosatrienoic acid). Gamma-linolenic acid (18:3 6Z,9Z,12Z) and dihomo-gamma-linolenic acid (20:3 8Z,11Z,14Z) are transformed into mixtures of conjugated diene and triene fatty acids, linoleic acid is only transformed to a conjugated diene.
Q8W257
O30564
NAGB_BORBU
Glucosamine-6-phosphate isomerase
Borreliella
MRLIIRPTYEDISKWAANHVAQKINEFSPTKENPFILGLPTGSSPIGMYKNLIELNKNKKISFQNVITFNMDEYIGIEENHPESYHSFMWNNFFSHIDIKKENINILNGNASNLKKECEEYEKKIKSFGGIMLFVGGIGPDGHIAFNEPGSSLTSRTRIKTLTQDTIIANSRFFEGDVNKVPKNALTVGIGTIMDSQEVLIIVNGHNKARALKHAIEKGVNHMWTISALQLHKNAIIVSDKNATYELKVGTVEYFNDIERKNFNNDLK
Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
O30564
Q47316
IUCA_ECOLX
Aerobactin synthase IucA
Escherichia
MILPSEKSATDVAAQCFLNALIRETKDWQLAEYPPDELIIPLDEQKSLHFRVAYFSPTQHHRFAFPAHLVTASGSYPVDFTTLSRLIIDKLRHQLFLPVPLCETFHQRVLESYAHTQQTIDARHDWAILREKALNFGEAEQALLTGHAFHPAPKSHEPFNRQEAERYLPDMAPHFPLRWFSVDKTQIAGESLHLNLQQRLTRFAAENAPQLLNELSDNQWLFPLRPWQGEYLFQQVWCQALFAKGLIRDLGEAGTSWLPTTSSRSLYCATSRDMIKFSLSVRLTNSVRTLSVKEVERGMRLARLAQTDGWQMLQARFPTFRVMQEDDWTGLRDLNGNIMQESLFSPAWKTLLLEQPQSQTNVLVSLTQAGPHGGDSLLVSAVKRLSDRLGITVQQAAHAWVDAYCQQVLKPLFTAEADYGLVLLAHQQNILVQMLGDLPVGFIYRDCQGSAFMPHATEWLDTIDEAQAENIFTREQLLRYFPYYLLVNSTFAVTAALGAAGLDSEANLMARVRTLLAEVRDQVTHKTCLNYVLESPYWNVKGNFFCYLNDHNENTIVDPSVIYFDFANPLQAQEV
Catalyzes the attachment of a first N-acetyl-N-hydroxylysine to a carboxylic group of citric acid to yield N-citryl-N-acetyl-N-hydroxylysine. Involved in the biosynthesis of the siderophore aerobactin which is a chelator that mediates the high-affinity iron transport systems induced under iron-stressed conditions.
Q47316
C0ZG90
SEPF_BREBN
Cell division protein SepF
Brevibacillus
MGVMNKLMGFLGLENEEYIEETTTVEEEREEQESSHKRQPAISRTNNVVPFQAREKEGIRLILCEPRHYSDAQDIADNLRHRRPVVVNLHRVEKDQAKRIIDFLSGTVYALNGDIQKVGDTIFVCTPDHVDIQGTISSVLEE
Cell division protein that is part of the divisome complex and is recruited early to the Z-ring. Probably stimulates Z-ring formation, perhaps through the cross-linking of FtsZ protofilaments. Its function overlaps with FtsA.
C0ZG90
P33296
UBC6_YEAST
Ubiquitin-protein ligase UBC6
Saccharomyces
MATKQAHKRLTKEYKLMVENPPPYILARPNEDNILEWHYIITGPADTPYKGGQYHGTLTFPSDYPYKPPAIRMITPNGRFKPNTRLCLSMSDYHPDTWNPGWSVSTILNGLLSFMTSDEATTGSITTSDHQKKTLARNSISYNTFQNVRFKLIFPEVVQENVETLEKRKLDEGDAANTGDETEDPFTKAAKEKVISLEEILDPEDRIRAEQALRQSENNSKKDGKEPNDSSSMVYIGIAIFLFLVGLFMK
Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. Cognate E2 conjugating enzyme for the DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains.
P33296
P37749
WBBI_ECOLI
GalF transferase
Escherichia
MYFLNDLNFSRRDAGFKARKDALDIASDYENISVVNIPLWGGVVQRIISSVKLSTFLCGLENKDVLIFNFPMAKPFWHILSFFHRLLKFRIVPLIHDIDELRGGGGSDSVRLATCDMVISHNPQMTKYLSKYMSQDKIKDIKIFDYLVSSDVEHRDVTDKQRGVIYAGNLSRHKCSFIYTEGCDFTLFGVNYENKDNPKYLGSFDAQSPEKINLPGMQFGLIWDGDSVETCSGAFGDYLKFNNPHKTSLYLSMELPVFIWDKAALADFIVDNRIGYAVGSIKEMQEIVDSMTIETYKQISENTKIISQKIRTGSYFRDVLEEVIDDLKTR
Involved in the transfer of galactofuranose (Galf) onto an alpha-D-gluco-configured acceptor substrate to form a beta-1,6-linkage. It uses n-octyl alpha-D-glucopyranoside as an acceptor substrate for the addition of galactofuranose from the donor substrate UDP-galactofuranose. It is not able to use beta-D-glucopyranoside isomers.
P37749
B6J7V3
NADK_COXB1
ATP-dependent NAD kinase
Coxiella
MLKIVSKPSFNRIALMGREGVEGVPETLAALKDYLVSLNREVILEENAAHMIDGSRLLTVPANDLKKKADLLIVVGGDGSLLNAAHIAVPQQLPVLGINRGRLGFLTDIPPNELTQISDILDGHYREEVRFLLEGTVEEGDEIVAQGIALNDIVLLPGNAPKMIEFDIFINDEFVCNQRADGLIITTPTGSTAYALSGGGPILHPQLNAMALVPMFPHTLSSRPIVVDAESQIKITISPENDVSPYVSNDGQERVSIKPGGNVYTRKYHYPLHLIHPTDYNYYGTLRRKLDWEKRAAKV
Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
B6J7V3
Q92374
RFA3_SCHPO
Single-stranded DNA-binding protein P12 subunit
Schizosaccharomyces
MERPTPRVTKDMLPECSGKTVRIVGKANQVEGETAKVDSNGSFDMHLTVDNTLEPNHFYEFVVSVKPDSSVQLLTCVDFGTDIDMEVYQKLVLFSHKYNSLFFE
As part of the replication protein A (RPA/RP-A), a single-stranded DNA-binding heterotrimeric complex, may play an essential role in DNA replication, recombination and repair. Binds and stabilizes single-stranded DNA intermediates, preventing complementary DNA reannealing and recruiting different proteins involved in DNA metabolism.
Q92374
Q93YP7
COQ2_ARATH
Polyprenyltransferase 1
Arabidopsis
MAFFGLSRVSRRLLKSSVSVTPSSSSALLQSQHKSLSNPVTTHYTNPFTKCYPSWNDNYQVWSKGRELHQEKFFGVGWNYRLICGMSSSSSVLEGKPKKDDKEKSDGVVVKEASWIDLYLPEEVRGYAKLARLDKPIGTWLLAWPCMWSIALAADPGSLPSFKYMALFGCGALLLRGAGCTINDLLDQDIDTKVDRTKLRPIASGLLTPFQGIGFLGLQLLLGLGILLQLNNYSRVLGASSLLLVFSYPLMKRFTFWPQAFLGLTINWGALLGWTAVKGSIAPSIVLPLYLSGVCWTLVYDTIYAHQDKEDDVKVGVKSTALRFGDNTKLWLTGFGTASIGFLALSGFSADLGWQYYASLAAASGQLGWQIGTADLSSGADCSRKFVSNKWFGAIIFSGVVLGRSFQ
Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate. Required for embryo development.
Q93YP7
C5BV49
UVRB_BEUC1
Excinuclease ABC subunit B
Beutenbergia
MRPVTDLQRRVFPFEVISDFTPSGDQPDAIAQLTARLQAGEKDIVLLGATGTGKSATTAWLIEQVQRPTLVMAPNKTLAAQLATEFRELLPNNAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSINDEVERLRHSATNSLLTRRDVVVVASVSCIYGLGTPQEYVDRMVRLRVGMQIERDDLLRQFVGMQYTRNDLSFQRGTFRVRGDTVEIIPVYEELALRIEFFGDEVEAIHTLHPLTGDVVRAEEEMYLFPATHYVAGPERMERAIAGIEVELEDRLAELEGGGRLLEAQRLRMRTTYDIEMMRQIGTCSGIENYSRHIDGREPGSPPHTLLDYFPEDFMLVIDESHQTVPQIGAMYEGDSSRKRTLVEHGFRLPSAMDNRPLRWEEFLERIGQTVYLSATPGPYELGQSDGVVEQVIRPTGLVDPEIVVKPTKGQIDDLLAEINARAERDERVLVTTLTKKMSEDLTDYLLERGVRVRYLHSEVDTLRRVELLRELRTGVFDVLVGINLLREGLDLPEVSLVAILDADKEGFLRSGTSLIQTIGRAARNVSGQVHMYADSVTPSMALAIEETNRRREKQVAYNTERGIDPEPLRKRIGDITELLAREDIDTKELLAGGYRQAGSKAPVPRKAGGDGSMRERLAGAATADLAELIQELTDQMHVAAGELQFEVAARLRDEISDLKKELRQMSAASA
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
C5BV49
P12003
VINC_CHICK
Metavinculin
Gallus
MPVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDLTAPVSAVQAAVSNLVRVGKETVQTTEDQILKRDMPPAFIKVENACTKLVRAAQMLQADPYSVPARDYLIDGSRGILSGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLVTYTKNLGPGMTKMAKMIDERQQELTHQEHRVMLVNSMNTVKELLPVLISAMKIFVTTKNTKSQGIEEALKNRNFTVEKMSAEINEIIRVLQLTSWDEDAWASKDTEAMKRALALIDSKMNQAKGWLRDPNAPPGDAGEQAIRQILDEAGKAGELCAGKERREILGTCKTLGQMTDQLADLRARGQGATPMAMQKAQQVSQGLDLLTAKVENAARKLEAMTNSKQAIAKKIDAAQNWLADPNGGSEGEEHIRGIMSEARKVAELCEEPKERDDILRSLGEISALTAKLSDLRRHGKGDSPEARALAKQIATSLQNLQSKTNRAVANTRPVKAAVHLEGKIEQAQRWIDNPTVDDRGVGQAAIRGLVAEGRRLANVMMGPYRQDLLAKCDRVDQLAAQLADLAARGEGESPQARAIAAQLQDSLKDLKARMQEAMTQEVSDVFSDTTTPIKLLAVAATAPSDTPNREEVFEERAANFENHAARLGATAEKAAAVGTANKTTVEGIQATVKSARELTPQVVSAARILLRNPGNQAAYEHFETMKNQWIDNVEKMTGLVDEAIDTKSLLDASEEAIKKDLDKCKVAMANMQPQMLVAGATSIARRANRILLVAKREVENSEDPKFREAVKAASDELSKTISPMVMDAKAVAGNISDPGLQKSFLDSGYRILGAVAKVREAFQPQEPDFPPPPPDLEHLHLTDELAPPKPPLPEGEVPPPRPPPPEEKDEEFPEQKAGEAINQPMMMAARQLHDEARKWSSKPVTVINEAAEAGVDIDEEDDADVEFSLPSDIEDDYEPELLLMPTNQPVNQPILAAAQSLHREATKWSSKGNDIIAAAKRMALLMAEMSRLVRGGSGNKRALIQCAKDIAKASDEVTRLAKEVAKQCTDKRIRTNLLQVCERIPTISTQLKILSTVKATMLGRTNISDEESEQATEMLVHNAQNLMQSVKETVREAEAASIKIRTDAGFTLRWVRKTPWYQ
Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion.
P12003
Q6DGJ1
GRIFN_DANRE
Galectin-related inter-fiber protein
Danio
MTLRFEASCPDGLCPGWSVILKGETPPEASKFEINFLCDRDDRVAFHFNPRFTESDIICNSYMANRWGQEERCNHFPLGVEEPFQIEIYSDNDHFHVYIDKAKVMQYKHRVEDLKTITKLQVVNDVKISSLEITKKLFY
Binds lactose.
Q6DGJ1
A4XXZ2
FOLD2_PSEMY
Methenyltetrahydrofolate cyclohydrolase
Pseudomonas
MSAVLSPKLIDGKAAAARVLAEVTEDVRTLKAAGIKPALAVVLVGDDPASQVYVRNKVLRAEECGIRSLEHKLPADTAEADLLALIHSLNADYSVHGILVQLPLPAHIDETRVLQAINPLKDVDGFHAENVGGLSQGRDVLTPCTPAGCLRLLQDSCGDLTGKHAVVIGRSNIVGKPMAALLLKAHCSVSVVHSKSANLRELCRQADIVVAAVGKPRLVDADWLKPGAVVIDVGINRIDEGGRSRLVGDVDFDSALTRAAAITPVPGGVGPMTIAFLMKNTLVAARLQHPATGLPLSTLENPA
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
A4XXZ2
Q7YRP2
VN1R4_PONPY
V1r-like receptor 4
Pongo
MASRYVAVGMMLSQTVVGVLGSFSLLLHYLSLHYIGCRLRSADLIVKHLIAASFLTLLCKGVPQTMAAFRVRYFLNAIGCKLVFYLHRVGRGVSTGTTCLLSVFQVITVSSRKSRWAKLKEKAPKHVGFSVLLCWILCMLVNIIFPIYVTGKRNHTNITVNKDLGDCCGRGNNKIAQTLRAMLLSFPDVLCLGFMLWASSSMVCILHRHKQRVQHIHRSNLSPRASPENRATQSILIPVSTFVSSYTLSCLLQVCMALLDNPNSLLVNTSALMSACFPTLSPFVLMSCDPSVYRLCFAWKR
Putative pheromone receptor.
Q7YRP2
A7I464
CDC6_METB6
ORC1-type DNA replication protein
Methanoregula
MPETEDPATGLFIKYLSNNRIFRDREVLRHSYRPQILPHRQPQIDTIASILAPSLRNETPSNILIYGKTGTGKTASVRYVGSELEKASSTMGTTCRIVHLNCEVIDTQYRVLAQIAKCIDDVDEASSDKAKIHIPMTGWPTDQVYSELKNQLDTGGGVLVIVLDEIDKLVKKSGDDTLYNLTRINSDLKNSKVSIIGISNDLSFKDFLDPRVLSSLSEEEIVFPPYNAPQLVDILTQRAAGAFLDGAIADGVIPLCSALAAQEHGDARRALDLLRISGELADRDESKQVTDVHVKQAQAKIETDSMIECIATLPTQSKLILFSMLTLEQLGQNIFTSGEVSRVYQDIAPEIQLDILTHRRITDLISELNMLGVINTRVVSRGRYGRTKEMWFDANTGKIREVVLKDPRLNGLKDLDINQMETKWLKTWFR
Involved in regulation of DNA replication.
A7I464
Q5QZ35
NTPPB_IDILO
7-methyl-GTP pyrophosphatase
Idiomarina
MTLPLILGSGSKYRREILDRLHLNYDVVKPDIDESAISSESPQQLVGRLAEAKARAVEKRMTYDNAIIIGSDQVAVCDGNILGKPGNRENAVRQLSSFIGKTVTFYTGLAVFNTEAQQCEVRVEPFEVEFRQLTAEEIERYVELENPFDCAGSFKSEGLGISLFSGLKGNDPNTLIGLPAIALLDMLRTHGINPLNKD
Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Q5QZ35
P57371
TOP1_BUCAI
Untwisting enzyme
Buchnera
MQKSLVIVESPAKAKTINQYLGSEYIVKSSIGHIRDLTKGKLYNKEKNKKFLNENFIEKTNENKILIKQMGIDPYQNWKFEYHILPGKEKIISELKYIANQVKHIYLATDLDREGEAIAWHLKEVIGGDSSKFSRVVFNEITQHSIQKAFKNVGHINMNRVHAQQARRFMDRIVGYMISPLLWKKIARGLSAGRVQSVAVRIIADRESIIKNFVPEEYWKLDVSLISQDKKKINMDVTHYNNKKFRPINENEVSFAVEKIQKSSCIVKNYEEKISYLKAPAPFITSTLQQSASLRLGFSVKKTMFLAQKLYEEGYITYMRTDSNYLSEYAIKKVRKYIKSNYGSNYLPKEPNIYSNEKHSQEAHEAIRPSDIKIKNIDSDHLNSSAKKLYELIWNQFLASQMKSVKYKSITVTVLADMFKLQKSERIVMFQGWNKVLIEEKNVFSQFPILQTGSQLFINKVTPSQKFTKPPPRFSEASLVRELEKKGIGRPSTYSAITSKIQDRGYVKIKKNKFYAEKMGEILTIRLKKSFSNLIDYNFTAHMEKKLDQVAENKVTWRYLLDDFFKKFSEQLEQAKKSPEEGGMELNNIVPTSLNCPICCKKMGIKTAITGVFLSCLGYNNTDNKKRCKKTINLITLNDFNKEQDNQKKISLQLIQKCDICNMYMDSYFINEKLKLHICANNPSCSGYKFEKGVFKSPIYLSKTIQCEKCYNNMKLKIGPFGKFFTCINKICKNTRKILPNGEISDPKLEPIPFPELLCKQSDAWFVLREGISGIFFAANTFPKSRETRSPFVEELVRFQHLLPEKIYYLSSAPVIDNYGNKTIVCFDKKKKTHYIASKKDGKFTGWSAVFIDQKWCVINK
Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.
P57371
Q2SJX0
MIAA1_HAHCH
Isopentenyl-diphosphate:tRNA isopentenyltransferase 1
Hahella
MSIANDNPNARPVVVLGPTACGKTRLAVALARAFAGEVVSADSRQVFRGMDIGTGKDLQDYGDTPYHLIDIVDPGAPFSLFDYLGAMQRTLDDLDAREKRPIIAGGSGLYLDAILRGYRLVEAPVDPLLRERLKHHDQERLNALLASLRPLHNTTDTQDRERTLRAIEIAYAELNEDSPSVQISIDPVVIGLHCDNDRLRARIRERLETRLDEGLIEEVESLRAEGLSWRQLDELGLEYRYVALYLQEQLNRNDMMQKLASAIYLFARQQVKWFRRMERQGVAIHWLEADDAPLDNALALLRR
Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Q2SJX0
B1JFU0
ATPE_PSEPW
F-ATPase epsilon subunit
Pseudomonas
MAMTVHCDIVSAEGEIFSGLVEMVVAHGNLGDLGIAPGHAPLITNLKPGPITLTKQGGAQEVYYISGGFLEVQPNMVKVLADTVQRATDLDEAQAQEALKAAENALSLKGADFDYGAAAARLAEAAAQLRTVQQMRKGK
Produces ATP from ADP in the presence of a proton gradient across the membrane.
B1JFU0
Q88J01
UREF_PSEPK
Urease accessory protein UreF
Pseudomonas
MNSDLALLRLLQLASPGLPVGGFTYSQGLEWAVEAGWVRGVDSFAGWQREQVHDTLACLDWPVLARLYHACQAKDAEAFGHWSRFLLANRETAELRLEEQQRGAALARLLDGWQLGQAPAWRASLELTQLGGMAWLAAHWAIPLRQLALGHGFAWLEGAVMAGVKLVPFGQQAAQTLLRDLGADLPAALDQALALGDDQLGGGLPLLAIASSRHETQYTRLFRS
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
Q88J01
B3PKB3
RLMM_CELJU
23S rRNA 2'-O-ribose methyltransferase RlmM
Cellvibrio
MNQLFLHCRPGFEKECAAEITELAAAQGIYGYSKTKDNAAFVVFITQDERGAETLIRQLPFQSLIFVRQWFAGFGNLSDLPVTDRVSPLLEAARALPKTSDLTGETVDTNEGKALSALVKKFLLPFGKALDAHKCLDRKSPWRLHLVFLSGTEAYLGVAPVNNSSAWPMGIPRLRLPKSAPSRATLKLEEAWHHFIPAADWDRRLAPGMRAVDLGAAPGGWTWQLVQRSIYVEAIDNGPMDKDLLDSGLVTHVLADGFLFEPKKPVDWLVCDIVDKPARVSSMVIKWFSKGHCRQAIFNLKLPMKQRYMEVQKCRTRILGELGSLGMRAELDFKQLYHDREEVTGYLRVF
Catalyzes the 2'-O-methylation at nucleotide C2498 in 23S rRNA.
B3PKB3
Q0BI73
MNMA_BURCM
tRNA-specific 2-thiouridylase MnmA
Burkholderia cepacia complex
MTKRRVVVGMSGGVDSSVTAWLLKEQGYDVVGLFMKNWEDDDDGEYCSTRQDWIDVVSVADLIGIDVEAVNFAAEYKDRVFAEFLREYSAGRTPNPDVLCNAEIKFKAFLDHAMSLDAEMIATGHYARVRERDGRFELLKAFDHTKDQSYFLHRLNQAQLSKTMFPLGEIPKTKVREIAAQIGLPNAKKKDSTGICFIGERPFRDFLNRYLPTKPGPMKTPDGKVIGEHIGLAFYTFGQRKGIGLGGSKDGSGEPWFVAAKDIASNTLYVVQGHDHPWLLSRQLVAGNVSWVAGEPPADGFSCGAKTRYRQADAACSFGRADGERFSLAFDDAQWAVTPGQSAVLYDGEICLGGGIIEFAATGQPGQTAPAPAAGHTGALAEAR
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Q0BI73
Q9PLI3
NQRF_CHLMU
NQR-1 subunit F
Chlamydia
MSWLSSLYPIFIASTAFCALGLLLVAIILLSRKFLIKVHPCKLRINNDDSLTKTVDSGKTLLSSLLDSGIAIPSPCGGKAACKQCKIRITKNVDEPLETDRSTFSKQQLEQGWRLSCQTKVQHDMNLEIEERYFNASSWEGTVVSNENVATFIKELVLSVDPARPIPFKPGGYLQITVPSYKTNTSDWKQTMDPQYYSDWETFHLFDKVIDHQSLDANSANKAYSLASYPAELPLIKFNIRIATPPFINKSPDPTIPWGVCSSYIFSLKPGDKVTVSGPYGESFMKEDNRPVIFLIGGAGSSFGRSHILDLLLSKHTNRELTLWYGARSLKENIYQEEYEKLEKEFPNFHYHLVLSQPLQEDLDKGWDSKDPIKTNFLFKAFELGQLSKLPNPEDYLYYVCGPALHNSSILTLLDNYGVERSSIILDDFGS
NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. The first step is catalyzed by NqrF, which accepts electrons from NADH and reduces ubiquinone-1 to ubisemiquinone by a one-electron transfer pathway.
Q9PLI3
Q9EQN9
S19A2_MOUSE
Solute carrier family 19 member 2
Mus
MDVPARVSRRAAAAAARMLLRTARVPRECWFLPTALLCAYGFFANLRPSEPFLTPYLLGPDKNLTERQVYNEIYPVWTYSYLLLLFPVFLATDYLRYKPVILLQGLSLIVTWFMLLYAQGLLAIQFLEFFYGIATATEIAYYSYIYTVVDLGMYQKVTSYCRSATLVGFTVGSVLGQILVSVVGWSLFSLNVISLTCVSVAFAVAWFLPMPQKSLFFHHIPSSCHGVNGLKVQNGGIVTDTPAANHLPGWEDIESKIPLNLDEPPVEEPEEPKPDRLRVFRVLWNDFLMCYSSRPLLCWSVWWALSTCGYFQVVNYAQGLWEKVMPSQNADIYNGGVEAVSTLLGASAVFAVGYIKLSWSTWGEMTLFLCSLLIAAAVYVMDTVQSIWVCYASYVVFRIIYMVLITIATFQIAANLSMERYALVFGVNTFIALALQTLLTLIVVDARGLGLCITTQFLIYASYFAAISVVFLANGIVSIIKKCRKQEDPSSSPQASTS
High-affinity transporter for the intake of thiamine . Essential for spermatogenesis .
Q9EQN9
Q7U5U4
SURE_PARMW
Nucleoside 5'-monophosphate phosphohydrolase
Parasynechococcus marenigrum
MRVLISNDDGVFAEGIRTLAAAAVARGHDVTVVCPDQERSATGHGLTLQTPIRAERADELFVPGVTAWACSGTPADCMKLALFELVKDKPDLVLSGINHGPNLGTDVFCSGTVAAAMEGTLEGIPSMAISSACFQWRQFQAGAELAVEVAEQALADQWPENLLLNLNIPPCNRDAMGPLRWTRLSIRRYDEQFSSRVDPRGRAYYWLAGEVVNDLESAGEGPRDWPSDVAQIHANSPSLTPIQPDLFWRGSLSGLPQLKLKDQLVR
Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
Q7U5U4
P58170
OR1D5_HUMAN
Olfactory receptor 17-31
Homo
MDGDNQSENSQFLLLGISESPEQQRILFWMFLSMYLVTVLGNVLIILAISSDSHLHTPMYFFLANLSFTDLFFVTNTIPKMLVNFQSQNKAISYAGCLTQLYFLVSLVTLDNLILAVMAYDRYVATCCPLHYVTAMSPGLCVLLLSLCWGLSVLYGLLLTFLLTRVTFCGPREIHYLFCDMYILLWLACSNTHIIHTALIATGCFIFLTPLGFMTTSYVRIVRTILQMPSASKKYKTFSTCASHLGVVSLFYGTLAMVYLQPLHTYSMKDSVATVMYAVLTPMMNPFIYRLRNKDMHGAPGRVLWRPFQRPK
Odorant receptor.
P58170
Q02TY0
SAHH_PSEAB
S-adenosyl-L-homocysteine hydrolase
Pseudomonas
MSAVMTPAGFTDYKVADITLAAWGRRELIIAESEMPALMGLRRKYAGQQPLKGAKILGCIHMTIQTGVLIETLVALGAEVRWSSCNIFSTQDQAAAAIAAAGIPVFAWKGETEEEYEWCIEQTILKDGQPWDANMVLDDGGDLTEILHKKYPQMLERIHGITEETTTGVHRLLDMLKNGTLKVPAINVNDSVTKSKNDNKYGCRHSLNDAIKRGTDHLLSGKQALVIGYGDVGKGSSQSLRQEGMIVKVAEVDPICAMQACMDGFEVVSPYKNGINDGTEASIDAALLGKIDLIVTTTGNVNVCDANMLKALKKRAVVCNIGHFDNEIDTAFMRKNWAWEEVKPQVHKIHRTGKDGFDAYNDDYLILLAEGRLVNLGNATGHPSRIMDGSFANQVLAQIHLFEQKYADLPAAEKAKRLSVEVLPKKLDEEVALEMVKGFGGVVTQLTPKQAEYIGVSVEGPFKPDTYRY
May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.
Q02TY0
Q2TBL4
RPC3_BOVIN
DNA-directed RNA polymerase III subunit C
Bos
MTQAEIKLCSLLLQEHFGEIVEKIGVHLIRTGSQPLRVIAHDTGTSLDQVKKALCVLIQHNLVTYQVHKRGVVEYEAQCNRVLRMLRYPRYIYTAKTLYSDTGELIVEELLLNGKMTMSAVVKKVADRLTETMEDGKTMDYAEVSNTFVRLVDTHFVQRCPLVPATENSDTGPPPPAPTLVVSEKDMYLVPKLSLIGKGKRRRSSDEDATGEPKAKRPKQTTDNKEPIPDDGIYWQANLDRFHQHFRDQAIVSAVANRMDQTSSEIVRTMLRMSEVTTPSGAPFTQPLSSNEIFRSLPVGYNISKQVLDQYLTLLADDPLEFVGKSGDSGGGMYVINLHKALGSLATATLESVVQERFGSRCARIFRLVLQKKHLEQKQVEDFAMIPAKEAKDMLYKMLSENFISLQEIPKTPDHAPSRTFYLYTVNILSAARMLLHRCYKSVANLIERRQFETKENKRLLEKSQRVEAIIASMQATGAEEAQLQEIEEMITAPERQQLETLKRNVNKLDACEIQVDETIFLLESYIESTMKR
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. May direct with other members of the subcomplex RNA Pol III binding to the TFIIIB-DNA complex via the interactions between TFIIIB and POLR3F. May be involved either in the recruitment and stabilization of the subcomplex within RNA polymerase III, or in stimulating catalytic functions of other subunits during initiation. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts induce type I interferon and NF-Kappa-B through the RIG-I pathway. Preferentially binds single-stranded DNA (ssDNA) in a sequence-independent manner.
Q2TBL4
B4EWY5
FRDC_PROMH
Quinol-fumarate reductase subunit C
Proteus
MTTKRKPYVRGMQPNWWTKLGFYRFYITREGTCLPQLWFSLVVLFGVFALKNGPESWAGFVGFLSNPIVMLINIVTLIATVFHTATWFKLAPKAVNIVVKDEKLPQEPIVRGLWGLTIVVTVVILAVALIV
Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; fumarate reductase is used in anaerobic growth, and succinate dehydrogenase is used in aerobic growth. Anchors the catalytic components of the fumarate reductase complex to the cell inner membrane, binds quinones.
B4EWY5
Q2QD30
YCF2_CUCSA
Protein Ycf2
Cucumis
MKGQQFKLWILEFREIKNSHYFLDSWTQFNSLGSFIHIFFHQERFIKLLDSRIWSILLSRNSQGSTSNRYFTIKGVVLFVVAVVLIYRINNRKMVERKNLYLTGFLPIPMNFIGPRNDTLEESFGSSNINRLIVLLLYLPTSFVQVTDSSQLKGSSDQSRDHFDSISNEDSEYHTLINQKEIQQPLPEEIEEFLGNPTRSIRSFFSDRWSELHMGSNPIERSTRDQKLLKKEQDVSFVPSRRSENKEIVNIFKIITYLQNTVSIHPISSDPGCDMVPKDELDMDSSNKISFLKKNPFIYLFHLFHDRNRRGYTLHHDFESEERFQEMADLFTLSITEPDLVYHKGFAFSIDSYGLDQKQFLNEVFNSRDESKKKYLLVLPPIFYEENDSFYRRIRKKWVRTSPGNDLEDPKQKIVVFASNNIMEAVNQYRLIRNLIQIQYYRYIRNVLNRFFLMNRSDRDLEYGIQRDQIGNDTLNHRTIMKYTINQHLSNFKKGQKKWFDPLILISRTERSMNRDPNAYRYKWSNGSKNFQEHFISEQKSHFHFQVVFDRLRINQYSIDWSEVIDKKDWSKSLRFFLSKLLVFLSKFLLFLSNSLPFFFVSFGNIPIHRSEIHIYELKGPNDRLCNQLLESIGLQIVHLKKLKPFLLDDHYTSQKSKFLINGGTISPFLFNKIPKWMIDSFDTRNNRRKSFDNTDSYFSMISHDQDNWLNPVKPFHRSSLISSFYKATRLRFLNNPHHFCFYCNKRFPFYVDYVEKARINNYDFTYGQFLNILFIRNKIFSLCGGKKKHAFLERDTISPIESQVSNIFIPNDFPQSGDERYNLYKSFHFPIRSNPFVRRAIYSIADISVTPLTEGQIVNFERTYCQPLSDMNLSDSEGKNLHQYLNFNSNMGLIHTPCSEKYLPSEKRKKQSLYRKKCLEKGQMYRTFQRDSAFSTLSKWNLFQTYMPWFFTSTGYKYLNLLFLDTFSDLLPILSSSPKFVSIFDDIMHRSDRSWRILRKKLCLPQWNLISEISIKCLPNLLLSEEMIHRNNESPSISTHLRSPNVREFLYSILFLLLIAVYLVRTHLLFVSRAYSELQTEFEKVKSLMIPSYMIELRKLLDRYPTYERNSFWLKNLFLVALEQLGDSLEEIWGSASGGGPAYGVKSIRSKKKDWNINLINLISIIPNPINRIAFSRNTRHLSHTSKEIYSLIRKNVNGDWIDDKIQSWVWNSDSIDDKEREFLVQFSTLTTEKRIDQILLSLTHSDHLSKNDSGYQMIEQPGVIYLRYLVDIQKKYLMNYKFNTSCLAERRTFLAHYQTITHSQTSCGANSFHFPSHGKLFSLRLALSPGILVIGSIGTGRSYLVKYLATNSYLPFITVFLNKFRDNKPKFIDDSDDDSDDIDDSGDIDDSDDIDRDLDIDTELELLTMMNALTMEMKLEIDQFYITLQFELIKAMSPCIIWIPNIHDLYVNKSSHLYFGLLVNYLYRDFERCSTTNILVIASTHIPQKVDPALIAPNKLNTCIKIRRLLIPQQRKHFFTLSYTRGFHLEKKMFHTNGFGSITMGSNVRDLVALTNEALSISITQRKSIIDTNIIRSALHRQTWDLRSQVRSVQDHGILFYQIGRALAQNVLLSNCSIDPISIYMKKKSCNEGGSYLYNWYFELETSMKKLTILLYLLNCSAGSVVQDLWSLSGPDEKNGITSYVLVENDSHLVHGLLEVEGALFGSSWTEKDCSRFDNDRVTLLLRPEPRNPLDMIQNGSSSIVDQIFLYQKYESKFEEGEGVLDPQQIEEDLFNHIVWAPRIWSPWGFLFDCIERPNELGVPYWARSFRGKRIIYDEEDELQENDSEFLQSGTVQYQTRDRSSKEQGFFLINQFIWDPADPLFFLFQDHPFVSVFSHREFFADEEMAKGLLTSQPAFPTSLEKRWFINIKNTQEKYVELLIHRQRWLRTRTNSSLSKSNGFFRSNTLSESYQYLSNLFLSNGTLLDQMTKTLLRKRWLFPDEMK
Probable ATPase of unknown function. Its presence in a non-photosynthetic plant (Epifagus virginiana) and experiments in tobacco indicate that it has an essential function which is probably not related to photosynthesis.
Q2QD30
Q5JDB8
PTH_THEKO
Peptidyl-tRNA hydrolase
Thermococcus
MFKYKQVIVARKDLKLSKGKFAVQVAHGAVTAAIKAQKEKPEWFKAWFHEGQKKVVVKAENLEELFKLKAEAEKLGLPTALIKDAGLTEIPPGTVTVLAIGPGPEEVVDKVTGHLKLL
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Q5JDB8
Q127X4
NUOC_POLSJ
NDH-1 subunit C
unclassified Polaromonas
MLSSFPVSATQLGDTIAAVLGDKVKSLKIALGEVTVTVGAADYLASAVLLRDAAGCRFEQLIDLCGLDYSEYKDGQYDGLRYCVASHLLSVSLNQRVRLKVFCPDDDFPVVDSVNGVWNSANWFEREAFDLYGIIFEGHNDLRRILTDYGFIGHPFRKDFPTTGYVEMRYDAEQKRVIYQPVTIEPREITPRVIREDNYGGLQ
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Q127X4
Q08091
CNN1_MOUSE
Calponin H1, smooth muscle
Mus
MSSAHFNRGPAYGLSAEVKNKLAQKYDHQREQELREWIEGVTGRRIGNNFMDGLKDGIILCEFINKLQPGSVKKVNESTQNWHQLENIGNFIKAITKYGVKPHDIFEANDLFENTNHTQVQSTLLALASMAKTKGNKVNVGVKYAEKQERRFEPEKLREGRNIIGLQMGTNKFASQQGMTAYGTRRHLYDPKLGTDQPLDQATISLQMGTNKGASQAGMTAPGTKRQIFEPGLGMEHCDTLNVSLQMGSNKGASQRGMTVYGLPRQVYDPKYCLNPEYPELSEPTHNHHPHNYYNSA
Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity.
Q08091
P52397
E13J_TOBAC
PR-37
Nicotiana
NSFINPIIQFLARNNLPLLANVYPYFGHIYNTADVPLSYALFTQQEANPAGYQNLFDALLDSMYFAVEKAGGPNVEIIVSESGWPSEGNSAATIENAQTYYRNLIDHVKRGAGTPKKPGKTIETYLFAMFDENDKKGEITEKHFGLFSPDQRAKYQLNFN
Implicated in the defense of plants against pathogens.
P52397
A7I841
PSB_METB6
Proteasome core protein PsmB
Methanoregula
MPEQYQESMTGTTTVGLVFAGGVILATEKRATMGYMIASKRAKKVYQIADRIGMTIAGGVGDAQQLARIITVECNLYQIRRSREITVGAASTLLSNYLNQNRYFPYYVQLLVGGIDDHGPSVYSVDAMGGATKEEDIVSTGSGSPMAYGVLEDRYRPGMNEDEAVELAVRALRSAMKRDAGSGEGIHVVVITKDRYENVSEETIKKHLAKTIA
Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
A7I841
P43386
GLNA_HALVD
Glutamine synthetase I alpha
Haloferax
MTEDNALTDGGLSDEAQAVIDEIEEKNVDFLRLQFTDILGTVKNVSIPASQAEKAFTEGIYFDGSSIDGFVRIQESDMRLEPDPSTFAVLPWRKKENSAAGRLICDVFNTSTGEPFSGDPRGVLKRAIERAEELGYDVNVAPEPEFFLFEEDEDGRATTVTNDAGGYFDLAPKDLASDVRRDIIYGLESMGFDIEASHHEVAEGQHEINFTYDDALSTADNVATFRSVVRAIAAEHDLHATFMPKPIPRINGSGMHTHISLFKDGENAFHDGDDEFDLSDTAKSFVAGILDHAPAITAVADPTVNSYKRLVPGYEAPVYIAWSDRNRSALIRKPAARTPAASRIEARFPDPSCNPYLAFAALIHAGLDGVEKGLDCPDPVRENIYEFDEAKREEYGIETLPKDLGGAVDALEEDEVIQEALGDHVFEKFVEAKRSEFKDYLVDVSQWELDRYLETF
Glutamine synthetase (GS) is an unusual multitasking protein that functions as an enzyme, a transcription coregulator, and a chaperone in ammonium assimilation and in the regulation of genes involved in nitrogen metabolism. It catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. Feedback-inhibited GlnA also interacts with and regulates the activity of the transcriptional regulator TnrA. During nitrogen limitation, TnrA is in its DNA-binding active state and turns on the transcription of genes required for nitrogen assimilation. Under conditions of nitrogen excess, feedback-inhibited GlnA forms a stable complex with TnrA, which inhibits its DNA-binding activity. In contrast, feedback-inhibited GlnA acts as a chaperone to stabilize the DNA-binding activity of GlnR, which represses the transcription of nitrogen assimilation genes.
P43386
A8ET60
DAPA_ALIB4
4-hydroxy-tetrahydrodipicolinate synthase
Aliarcobacter
MDIITGSMTALITPFKNGKVDLQKYESLIKRQIAQGINAVSPVGTTGESATLSHKEHKECIEVAVATCKNSGVKVLAGAGSNATHEACDIAKFAQEVGADGILSIAPYYNKPTQEGLYQHYKAIANSVELPLMLYNVPGRTGVDLLPETAIRLFDDVKNIYGIKEATGSLERATSLMSARKDFVVVSGDDSVDFPMLASGARGIISVTSNLLPNLKSKLVSSVLEGDYKTSLSIHNDLYELNKTLFCESNPIPIKAAMYLSGLLDSLEFRLPLTNPSAETMQKLEKILIKYEVIK
Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
A8ET60
C1B058
GLMM_RHOOB
Phosphoglucosamine mutase
Rhodococcus
MGRLFGTDGVRGLANTELTAELALQVASAAATVLASPGSGGRKTAVVGRDPRASGEMLEAAVVAGLTSAGVDVLNVGVLPTPAVAFLTAELDAALGVMISASHNPMPDNGIKIFAAGGHKLDDEVEDRIESVATGTATRRAPTGAGIGRVHTVPDAADRYLQHLTTALPNRLDGLTVVVDCAHGAASDVAPAAYRAAGATVVAINAEPDGLNINENCGSTHLEGLQKAVVRHGADLGLAHDGDADRCLAVDAGGSLVDGDAIMTVLALGMRDAGELVDDTLVATVMSNLGLHIAMREAGISLVTTAVGDRYVLEGLRSGGFSLGGEQSGHVVFPAFGTTGDGVLTGLRLMGRMAETGQPIAELASAMTTLPQVLVNVKVADKRAVAASPVVLDAVLAAERSLGENGRVLLRPSGTEQLVRVMVEASDLEVARKLADELAGTVASV
Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
C1B058
Q3E764
TMA7_YEAST
Translation machinery-associated protein 7
Saccharomyces
MSSRQGGKMKPLKQKKKQQQDLDPEDIAFKEKQKADAAAKKALMANMKSGKPLVGGGIKKSGKK
Involved in protein synthesis.
Q3E764
D4AK75
SED3_ARTBC
Sedolisin-C
Trichophyton
MLLRWHSVIPLFLAMTVAFPNTYRTVVEDLPAIPEGWVQGNPPSPETSVRMNLAVGQQNTRTFEQIVLDISTPGHRNYGKHLSRRDLKGLLRPRRETSNLILSWLEKSGVPKRSIVDDGDWIHFVISISQAERMLQTRFYHFHDVQDPGISMIRTLKYSVPSRLARHVYMIQPTTKFGKPKKHANSIANLQAIYLSTNATENCNATITPRCLRELYKMGDYVAKPDCRNVIGVSGYLDQYARYSDFYKFLELYAPEMKGANFSVAHIGNGQNLQNSTRNSIEASLDIEYALGLSNASAVFYTTSGRGPLVPDLDQPEQEHNSNEPYLDQLHYLLSLPQEALPAVLSTSYGENEQSVPERFSHATCNLFAQLGARGVSVIFSSGDSGVGSSCLTNDKKKITRFNPTFPASCPFVTSVGATFKINPERATGFSSGGFSDRHSRPGYQNDAVQHYLDKLGDRWKGLYNPKGRGIPDVSAQGANFAIYDHGKVIIVSGTSASAPAFAAIIANLNAIRLRANKPVLGYLNPFIYGKGREGFTDIVHGGSKGCVGYSSTNRSTPAVPYASWNATEGWDPVTGVGTPNFRILAKIVQHME
Secreted tripeptidyl-peptidase which degrades proteins at acidic pHs and is involved in virulence.
D4AK75
Q9PJZ0
NRDR_CHLMU
Transcriptional repressor NrdR
Chlamydia
MLCPFCNHGELKVIDSRNSPEANAIKRRRECLRCSQRFTTFETVELTIQVLKRDGRYENFQEAKLINGLKAASSHTRIGQEQVQAIASNIKQDLLGKQNREISTKEIGELVMKYLKKADMIAYIRFACVYRRFRDVGELMEVLLSATPDGEK
Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
Q9PJZ0
A7I4H6
RUVB_METB6
Holliday junction ATP-dependent DNA helicase RuvB
Methanoregula
MSERVISPEPVPDDADEITLRPSTLEAFVGQEPAKNALRIAIAAARKRGEPIDHILFAGPPGLGKTTLAHIIAREMGAAIRTTTGPVLEKTGDMAAIATALQNGDVLFIDEIHRMNPVVEEILYPAMEDFFIDVMIGEGPSARSIKLTLERFTLIGATTRQGLLSSPFRDRFGLLIRLNLYSPEDLEKIVTRSAEILRIPITPKGAAVIASRSRGTPRIANRLLRRVRDYAVVEGDGTITAEIAGAGLALLQIDELGLDDIDRRILSVIAGDFGGGPVGAKTIAISVGEEVRTIEEVYEPYLIQIGFVKRTPQGRETTPAALAHLKLNHSQKTLF
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.
A7I4H6
Q3C257
ACR1A_ACTEQ
Acrorhagin-1a
Actinia
MNQVMTIFLVLGVIVYSVESSLTPSSDIPWEKCRHDCFAKYMSCQMSDSCHNKPSCRQCQVTYAICVSTGCP
Toxin that is lethal to crab. It interacts with divalent metal ions (zinc and nickel) suggesting it may function as a metal ion chelator to regulate metal ion levels or as a metal ion transporter, or that its function is modulated by metal ions. Is not active against any of the voltage-gated potassium and sodium channels tested. In addition, it does not show activity in bacterial and fungal growth inhibitory assays as well as in hemolytic assays.
Q3C257
B7KGG9
ACKA_GLOC7
Acetokinase
Gloeothece citriformis
MKILVLNAGSSTQKSCLYDLTGDTLPQAPPKPIWKGDIDWTIATDHGLLEIKANGVEKKLNLSADDHLKGMSQMLDSLVQGETKVIDDLSEIEIVGHRVVHGGLNYTQATLITQEVKQTIADLIPLAPTHNPAHLEGIETVEKLLGNVPQLAVFDTAFHSTLPLEVAAYPLPYEWLEKGLRRYGFHGISHQYCVHRAAELLGKPLNSLKLINCHLGNGCSLAAVKDGISINTTMGFTPLEGLMMGSRSGSIDPEIPIFLIRDHGFTPEDVITVLNKKSGLKGVSGVSSDLRAIQKAIQEGNEKAQLAFKMYIHRLRFYIGAMLASLGGLDALIFTAGVGENSSEVREQACEAFGFLGLKLDQAKNESRPVDEDIATPDSKVRVLVIHTEEDWAIAKECWHQLTQK
Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
B7KGG9
Q7UXX6
SYS_RHOBA
Seryl-tRNA(Ser/Sec) synthetase
Rhodopirellula
MLDRKFILQNAQLVAENSAKRGVSVDVDAICRLEAERMDALKQAEELNRQANEVSKQIKSAKDNDERQELIAKGRSLREQKDAAGAAQDRLEAEILELQTILPNMTHPDVPEGGEHDANEIGRGKTPVPEMDFQPLDHLQLGEKHDLFDFEGGARVAGSGFYFLRNAAVRLDLALQQFAISHLAGKGFTPVSTPDLALTSVLQGTGFNPRGPETQIYSIENTELNLVATAEIPLGGMLSGQILASEELPLRYCGLSHCFRTEAGAAGRASKGLYRVHQFTKVEMFAFTLPDQSTAMHEEMRELECEIFDALEVPYRVIDTATGDLGGPAYRKYDLEAWMPGRGESGDWGEVTSTSNCTDYQARRLNVRSKSNTQKGTDFVHTLNGTAIATGRAMIAILENHQRADGTINVPEILRPWVGCDVLKCE
Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Q7UXX6
Q8N4N3
KLH36_HUMAN
Kelch-like protein 36
Homo
MMEGSRQTRVSRPYKISESSKVYRWADHSSTVLQRLNEQRLRGLFCDVVLVADEQRVPAHRNLLAVCSDYFNSMFTIGMREAFQKEVELIGASYIGLKAVVDFLYGGELVLDGGNIDYVLETAHLLQIWTVVDFCCEYLEQEVSEDNYLYLQELASIYSLKRLDAFIDGFILNHFGTLSFTPDFLQNVSMQKLCVYLSSSEVQRECEHDLLQAALQWLTQQPEREAHARQVLENIHFPLIPKNDLLHRVKPAVCSLLPKEANCEGFIEEAVRYHNNLAAQPVMQTKRTALRTNQERLLFVGGEVSERCLELSDDTCYLDAKSEQWVKETPLPARRSHHCVAVLGGFIFIAGGSFSRDNGGDAASNLLYRYDPRCKQWIKVASMNQRRVDFYLASIEDMLVAIGGRNENGALSSVETYSPKTDSWSYVAGLPRFTYGHAGTIYKDFVYISGGHDYQIGPYRKNLLCYDHRTDVWEERRPMTTARGWHSMCSLGDSIYSIGGSDDNIESMERFDVLGVEAYSPQCNQWTRVAPLLHANSESGVAVWEGRIYILGGYSWENTAFSKTVQVYDREADKWSRGVDLPKAIAGGSACVCALEPRPEDKKKKGKGKRHQDRGQ
Probable substrate-specific adapter of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Q8N4N3
Q8Z3X3
AC4CH_SALTI
N(4)-acetylcytidine amidohydrolase
Salmonella
MQPNDITFFQRFQNDILAGRKTITIRDASESHFKAGDALRVGRFEDDGYFCTIEVTGTSTVTLDTLNEKHAQQENMSLDELKRVIAEIYPNQTQFYVIDFKCL
Catalyzes the hydrolysis of N(4)-acetylcytidine (ac4C).
Q8Z3X3
Q39EE8
NUOD_BURL3
NDH-1 subunit D
Burkholderia cepacia complex
MAEIKNYTLNFGPQHPAAHGVLRLVLELDGEVIQRADPHIGLLHRATEKLAESKTFIQSVPYMDRLDYVSMMVNEHGYVLAIEKLLGIEVPERAQYIRVLFDEITRVLNHLMWIGAHALDVGAMAVFLYAFREREDLMDVYEAVSGARMHAAYYRPGGVYRDLPDAMPQYKASKIRNEKALAKMNEARSGSVLDFIDDFFARFPKCVDEYETLLTDNRIWKQRLVGIGVVSPERALQMGLTGPMLRGSGIAWDLRKKQPYEVYDRMDFDVPVGVNGDCYDRYLVRVEEMRQSIRIAKQCIEWLRKNPGPVMTDNHKVAPPSRVGMKTNMEDLIHHFKLFTEGFHVPEGEAYAAVEHPKGEFGIYLVSDGANKPYRLKIRAPGFAHLASLDEMARGHMIADAVTIIGTQDIVFGEIDR
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Q39EE8
Q7YRH4
RNAS9_PONPY
Inactive ribonuclease-like protein 9
Pongo
MMRTLITIHPLPLLLLLQQLLQPVQFQEVDTDYDLPEDKREEFEEYVEQFFSTGPTRPPTKEKVKRLLLIEPGMPLYHVDYCNSEIMRKNVYYKHRCVAEHYFLLMQYDELQKICYNRFVPCKNGVRKCNRSKGLVEGVYCNLTEAFRIPACKYESFYRKGYVLITCAWQNEMQKLIPHTINDLVEPPEHRSFLSEDGVFVISP
Does not exhibit any ribonuclease activity.
Q7YRH4
Q5XVG3
LAZY4_ARATH
Protein NEGATIVE GRAVITROPIC RESPONSE OF ROOTS 2
Arabidopsis
MKFFGWMQNKLHGKQEITHRPSISSASSHHPREEFNDWPHGLLAIGTFGNKKQTPQTLDQEVIQEETVSNLHVEGRQAQDTDQELSSSDDLEEDFTPEEVGKLQKELTKLLTRRSKKRKSDVNRELANLPLDRFLNCPSSLEVDRRISNALCDEKEEDIERTISVILGRCKAISTESKNKTKKNKRDLSKTSVSHLLKKMFVCTEGFSPVPRPILRDTFQETRMEKLLRMMLHKKVNTQASSKQTSTKKYLQDKQQLSLKNEEEEGRSSNDGGKWVKTDSDFIVLEI
Involved in the regulation of root gravitropism . Functions redundantly with LAZY2 and LAZY3 in the control of root gravitropism . Involved in the development of the root system architecture by influencing lateral root angles and primary root length . Functions redundantly with LAZY1, LAZY2 and LAZY3 to control plant architecture by coupling gravity sensing to the formation of auxin gradients . Involved in the establishement of auxin gradient in primary and lateral roots upon gravitropic stimulation . Involved redundantly with LAZY1 and LAZY2 in the regulation of both shoot and root gravitropism . Mediates gravity signaling in statocytes downstream of amyloplast displacement, leading to the generation of asymmetric auxin distribution in gravity-responding organs . Regulates the direction of polar auxin transport in response to gravity through the control of asymmetric PIN3 expression in the root cap columella . Regulation of auxin flow by the three proteins LAZY1, LAZY2 and LAZY4 in statocytes influences plant architecture by controlling the growth angle of lateral shoots and lateral roots .
Q5XVG3
Q85FK5
PSBE_ADICA
PSII reaction center subunit V
Adiantum
MSGNTGERPFADIITSIRYWVIHSITIPSLFIAGWLFVSTGLAYDVFGSPRPNEYFSESRQEVPLITGRFDSLEQVDAFTKSF
This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Q85FK5
A4G8S7
SECA_HERAR
Protein translocase subunit SecA
Herminiimonas
MSLLTQIFGSRNQRLLKQYQKTVREINALEPAMEQLSDAALQAKTPEFKERLAKGEDIDSILPEAFAVCREASKRVLKMRHFDVQLIGGMTLHYGKIAEMGTGEGKTLMATLPTYLNALTGKGVHVVTVNDYLAQRDAEWMGTLYGWLGLSTGVNMSQIDHDAKQIAYNSDITYGTNNEFGFDYLRDNMVYDTADRVQRDLHFAVVDEVDSILIDEARTPLIISGQAENHTELYHKINAVPPLLTLQIGEETPDGKGTVEVPGDYTKDEKAHQVLLTEAGHEKAEQILTRMGLLPEGASLYDAANITLIHHLYAALRAHTLYHKDQHYVVQNDEVVIVDEFTGRLMTGRRWSDGLHQAVEAKEGVRIQNENQTLASITFQNYFRMYSKLAGMTGTADTEAYEFQEIYGLETVVIPQNRPNQRKDRQDQVYKSSEEKYGAMLKDIQDCYERGQPVLVGTTSIENSELLSGILNKANLPHNVLNAKQHAREAEIIAQAGRPKAITIATNMAGRGTDIVLGGNVAKQVQIIEANDALSEAEKTAQAQKLGDEWQSLHDQVVAAGGLHIIGTERHESRRVDNQLRGRAGRQGDPGSSRFYLSLDDALLRIFAGDRVRAIMDRLKMPEGEPIEAGIVSRSIESAQRKVEARNFDIRKQLLEYDDVANDQRKVIYQQRNELLETQDVSELITSLRQGVFADLFRTYVPEQSMEEQWDLKALDEILRNEWQIDFSLAAVLEAEPNITDEEMLERLLQVTDAAYEAKVAIVGRESFAGFERGVMLQSVDSNWREHLAALDHLRQGIHLRGYAQKNPKQEYKREAFELFGQMLNLIKDAVVKTVMTVRIQSREEIDAAEEQLAQAHVENVHYQHADFDPDAAPEELLAPTAQAHEAASQPQVNTMPKVGRNDPCPCGSGKKYKQCHGRLA
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
A4G8S7
Q5FQD0
ARGJ_GLUOX
Arginine biosynthesis bifunctional protein ArgJ beta chain
Gluconobacter
MQLRLPHLQRSKSMAKPLPVSPLARPLPDLATIAGVRLSAVAAGIRYQGRTDLMLAEFVPGTVAAGVYTKNACPGAPVLWCREALTTPYARALLVNAGNANVFTGRAGIQACEDCADATAQLLDCPPQDVFLASTGVIGEKLPQDRIIAALPAARAGLEENGWADAARAIMTTDTFPKAARRDVKINGTPVRIQGIAKGSGMVAPDMATMLAYVATDAKLPQNVLQSLLASGCAQSFNSITVDSDTSTSDMLMIFATGLADNPEVDDVNDPALAEFTLALNDLLLELALMVVRDGEGATKLVRIAVTGADSNLSAHRIALCIANSPLVKTAIAGEDANWGRVVMAVGKSGEPADRDRLSVAIGGTWIAKDGGVVENYDEAPVVAHMKGQEIEIAVDLDLGDGQARVWTCDLTHGYIDINGSYRS
Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.
Q5FQD0
P52867
PMT5_YEAST
Dolichyl-phosphate-mannose--protein mannosyltransferase 5
Saccharomyces
MNKEHLLKVDPIPDVTIKRGPLRSFLITKPCDNLSSLRTVTSSKEKLLVGCLLIFTAIVRLHNISLPNSVVFGENEVGTFVSQYVNNIFFTDVHPPLVAMLYATVSSVFGYKGLFNYGNIGTEYTANVPYVAMRFFSATLGIVSVLVLYLTLRVSGVKIAVAAICAVCFAIENSFVTLSRFTLIEGPFVFFMACAVYFFRRSELYLPNSCKANKSLLAASIALGFAVSSKWAGLFTIAWAGIIVLWRVWFMIGDLSRPIGSSIKYMAFQFTCLLAIPAFIYFLIFSVHIKTLNVNGISSSFFPAEFRKTLKYNNVIKETVAEVAVGSAVSLNHVGTAGGYLHSHLHNYPAGSMQQQVTLYPHIDQNNKWIIELAEHPNENVTSFQNLTDGTIIKLRQLKNGCRLHSHDHKPPVSQNADWQKEVSCYGYEGFEGDINDDWIIEIDKKRSEPGPAQEHIRAIETKFRLKHYLTGCYLFSHPEKLPEWGFGQQEVTCAYFAREDLTSWYIEENENEISLPNPEKVSYKKMSFWQKFVAIHKFMFYLNNYMDTSHAYSSEPKTWPLMLRGIDFWNENGREVYFLGNAVLWWSVTAFICTFIIGVAVELLAWKLGVNILRDKHIINFHYQVFQYLLGFAAHYFPYFFVGQKLFLYDYLPAYYFGILAFGHALDLISTYISNKRNNTGYIVVAIFMVVCFYFFSEHSPLIYATGWSSNLCKRSKWLGSWDFYCNSLLLSDSHYELNAES
Protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Forms a heterodimeric complex with PMT3 and more rarely with PMT2 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins.
P52867
Q5ECE3
LOPAP_LONON
Prothrombin activator
Lonomia
MKFFGLFLAILASTAADVVIDGACPDMKAVSKFDMNAYQGTWYEIKKFPVANEANGDCGSVEYTPDNGLLKVRAGHVEDDIEKFVVGVLTKNAGTSDAELTLSVVVGDYVRVAPLWIVSTDYDNYAIGYSCKDYKKSNQHRVNIWILSRTKTLNESSKSTVNKFLKEHSKEFDQSKFVETDFSEKACFFKKSHVYTVPFGA
Serine protease. Activates thrombin by cleavage of prothrombin. Does not activate factor X. When injected into rats, causes thrombus formation, fibrinogen depletion, uncoagulable blood, decreased platelet count, inhibition of collagen-induced platelet aggregation, leukocyte infiltration in lungs, congestion and hemorrhage in renal glomeruli and necrosis in renal distal tubules. Causes increase in surface expression of ICAM-1 and E-selectin on human umbilical vein endothelial cells (HUVEC), but does not affect expression of VCAM-1, or the expression of mediators involved in coagulation and fibrinolysis systems (TF, vWF and t-PA). Increases expression of the platelet activation inhibitors NO and PGI2. Increases viability of HUVEC, and inhibits apoptosis.
Q5ECE3
P80271
HBB_CHEKU
Hemoglobin beta chain
Chelidonichthys
VEWTDFERATIQDIFSKMDYETVGPATLTRTVIVYPWTLRYFAKFGNICSTAAILGNKEIAKHGTTILHGLDRGVKNMDDIKNTYAELSKLHSEKLHVDPDNFRLLSDCLTIVVAAKMGKDFTGEVQAAFQKFLSVVVNSLGRQYH
Involved in oxygen transport from gills to the various peripheral tissues.
P80271
Q8G7B0
ATPD_BIFLO
F-type ATPase subunit delta
Bifidobacterium
MRGEASRIADRESRDSLAPKLRDTREDAWRIGNELFTITKVLDDSIQLERALTDPSRPVADKVAVLKELLGDNAHPMTMEIMTDLVSRRWSRARDIANAVEDFGVDAMMYYADATDATLQVSIELSELHSALLNLPVVRAKLYDYQATSEARVKLFREVFSGKTLNKVTMRLAEHATCNLRRRRYLETIQWLINKFSRHMGESMVTVTTATPLKKEQIKRLVEVYSAKVGRQVHINSVVDPTVLGGMRIQVGDEVTDNTVVAQLQNLHRKVQTEATPA
This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
Q8G7B0
A6X935
ITIH4_MOUSE
Inter alpha-trypsin inhibitor, heavy chain 4
Mus
MKSPAPAHMWNLVLFLPSLLAVLPTTTAEKNGIDIYSLTVDSRVSSRFAHTVVTSRVVNRADAVQEATFQVELPRKAFITNFSMIIDGVTYPGVVKEKAEAQKQYSAAVGRGESAGIVKTTGRQTEKFEVSVNVAPGSKITFELIYQELLQRRLGMYELLLKVRPQQLVKHLQMDIYIFEPQGISILETESTFMTPELANALTTSQNKTKAHIRFKPTLSQQQKSQSEQDTVLNGDFIVRYDVNRSDSGGSIQIEEGYFVHHFAPENLPTMSKNVIFVIDKSGSMSGKKIQQTREALVKILKDLSPQDQFNLIEFSGEANQWKQSLVQATEENLNKAVNYASRIRAHGGTNINNAVLLAVELLDRSNQAELLPSKSVSLIILLTDGDPTVGETNPTIIQNNVREAINGQYSLFCLGFGFDVNYPFLEKMALDNGGLARRIYEDSDSALQLQDFYHEVANPLLSSVAFEYPSDAVEEVTRYKFQHHFKGSEMVVAGKLQDQGPDVLLAKVSGQMHMQNITFQTEASVAQQEKEFKSPKYIFHNFMERLWALLTIQQQLEQRISASGAELEALEAQVLNLSLKYNFVTPLTHMVVTKPEGQEQFQVAEKPVEVGDGMQRLPLAAQAHPFRPPVRGSKLMTVLKGSRSQIPRLGDAVRASRQYIPPGFPGPPGPPGFPAPPGPPGFPAPPGPPLASGSDFSLQPSYERMLSLPSVAAQYPADPHLVVTEKSKESTIPEESPNPDHPQVPTITLPLPGSSVDQLCVDILHSEKPMKLFVDPSQGLEVTGKYENTGFSWLEVTIQKPHLQVHATPERLVVTRGRKNTEYKWKKTLFSVLPGLKMTMNMMGLLQLSGPDKVTIGLLSLDDPQRGLMLLLNDTQHFSNNVKGELGQFYRDIVWEPPVEPDNTKRTVKVQGVDYLATRELKLSYQEGFPGAEISCWTVEI
Type II acute-phase protein (APP) involved in inflammatory responses to trauma. May also play a role in liver development or regeneration.
A6X935
B1L0B3
RUVA_CLOBM
Holliday junction ATP-dependent DNA helicase RuvA
Clostridium
MYEYIKGKYIDMYKDYIVIENNNIGYKIYTSGSTMAKLPSIGENIMLYTEQIVREDFIGIYGFLTKDELSMFKLLLTINGVGAKAALSLLSISNVSTLKYAIKVGDEKTITRAPGIGKKTAQRIILELKDKIEIDISEEDDEQIINKVTDDKKVLEAVAALVTLGYSEKEASKVINLCDKNNSLEQIIKEALKHLMK
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB.
B1L0B3
A5UCU6
HEMH_HAEIE
Protoheme ferro-lyase
Haemophilus
MTKSAKIGVLLANLGTPDSPTPKSISRYLWQFLTDPRVVDLPRCKWYPLLKAIILPLRSKRIAKNYQAIWTEQGSPLLAISRQQKDALQAYLDTQNINAQVEIAMTYGNPSIQSAVKNLLKNQVERIIVLPLYPQYSSSTTGAVFDAFANALKEERGLVPFDFIHSYHIDENYINALANSIKVRLKSDEFLLFSYHGIPLRYEKMGDYYREHCKQTTIAVVNKLGLTENQWGMTFQSRFGREEWLQPYTDKFLESAATQNIQKIAVICPGFSVDCLETIEEIDKENRENFLKNGGQSYQYIPALNVEHAHIEMMGKLILEKLA
Catalyzes the ferrous insertion into protoporphyrin IX.
A5UCU6
P15788
FER_HALP7
Ferredoxin
unclassified Halothece
MASYKVTLINEEMGLNETIEVPDDEYILDVAEEEGIDLPYSCRAGACSTCAGKIKEGEIDQSDQSFLDDDQIEAGYVLTCVAYPASDCTIITHQEEELY
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
P15788
B9JMX8
THIG_AGRRK
Thiazole synthase
Agrobacterium tumefaciens complex
MLALYGTEVASRLLLGTARYPSPAILAEAVRQSATEIVTVSLRRETAGGRNGGAFFEMIRTLGVRILPNTAGCHGVSEAVLTAKMAREVFQTNWIKLEVIGNHDTLQPDVFGLVEAARILASEGFEVFPYTTDDLVVAERLLDAGCKVLMPWCAPIGSAAGPLNLSALRAMRAHFPDVPLIVDAGIGRPSHATTVMELGFDAVLLNTAVAGARDPAAMAGAFAKAIDAGRLAFTAGMLEPRDMAVPSTPVIGKAVFA
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.
B9JMX8
P28707
SBA1_YEAST
Co-chaperone protein SBA1
Saccharomyces
MSDKVINPQVAWAQRSSTTDPERNYVLITVSIADCDAPELTIKPSYIELKAQSKPHVGDENVHHYQLHIDLYKEIIPEKTMHKVANGQHYFLKLYKKDLESEYWPRLTKEKVKYPYIKTDFDKWVDEDEQDEVEAEGNDAAQGMDFSQMMGGAGGAGGAGGMDFSQMMGGAGGAGSPDMAQLQQLLAQSGGNLDMGDFKENDEEDEEEEIEPEVKA
Acts as a co-chaperone.
P28707
Q54450
HASA_SERMA
Heme acquisition system protein A
Serratia
MAFSVNYDSSFGGYSIHDYLGQWASTFGDVNHTNGNVTDANSGGFYGGSLSGSQYAISSTANQVTAFVAGGNLTYTLFNEPAHTLYGQLDSLSFGDGLSGGDTSPYSIQVPDVSFGGLNLSSLQAQGHDGVVHQVVYGLMSGDTGALETALNGILDDYGLSVNSTFDQVAAATAVGVQHADSPELLAA
Can bind free heme and also acquire it from hemoglobin. Conveys heme from hemoglobin to the HasR receptor which releases it into the bacterium. HasR alone can take up heme but the synergy between HasA and HasR increases heme uptake 100-fold.
Q54450
Q2NU15
MNMA_SODGM
tRNA-specific 2-thiouridylase MnmA
Sodalis
MSDNGQKKVIVGMSGGVDSSVSAWLLQQQGYRVEGLFMKNWEEDDNEEYCTAASDLADARAVCDTLGIALHTVNFAAEYWDNVFAHFLAEYQVGRTPNPDILCNKEIKFKAFLEFADDDLGADYIATGHYVRRADVNGKSRLLRGLDDNKDQSYFLYTLGHAQLARCLFPIGELAKPEVRRIAADLGLATAAKKDSTGICFIGERKFRDFLGRYLPVQPGAIVSVDGQEVGRHQGLMYHTLGQRKGLGIGGTRDGSEDPWYVVDKDLDHNRLIVAQGHQHPRLMSTGLTAGQLHWVEREPLTEALRCTVKIRYRQPDIACLVTPQADGRLQVTFDQPVTAVTPGQSAVFYLAERCLGGGIIEARQPLSH
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln), leading to the formation of s(2)U34, the first step of tRNA-mnm(5)s(2)U34 synthesis. Sulfur is provided by IscS, via a sulfur-relay system. Binds ATP and its substrate tRNAs.
Q2NU15
Q0SZ00
DAPF_SHIF8
PLP-independent amino acid racemase
Shigella
MQFSKMHGLGNDFMVVDAVTQNVFFSPELIRRLADRHLGVGFDQLLVVEPPYDPELDFHYRIFNADGSEVAQCGNGARCFARFVRLKGLTNKRDIRVSTANGRMVLTVTDDDLVRVNMGEPNFEPSAVPFRANKAEKTYIMRAAEQTILCGVVSMGNPHCVIQVDDVDTAAVETLGPVLESHERFPERANIGFMQVVKREHIRLRVYERGAGETQACGSGACAAVAVGIQQGLLDEEVRVELPGGRLDIAWKGPGHPLYMTGPAVHVYDGFIHL
Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Q0SZ00
P0A9Q0
IDNO_ECOL6
5-keto-D-gluconate 5-reductase
Escherichia
MNDLFSLAGKNILITGSAQGIGFLLATGLGKYGAQIIINDITAERAELAVEKLHQEGIQAVAAPFNVTHKHEIDAAVEHIEKDIGPIDVLVNNAGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVTRHMVERKAGKVINICSMQSELGRDTITPYAASKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTKALVEDEAFTAWLCKRTPAARWGDPQELIGAAVFLSSKASDFVNGHLLFVDGGMLVAV
Catalyzes the reduction of 5-keto-D-gluconate to D-gluconate, using either NADH or NADPH. Is likely involved in an L-idonate degradation pathway that allows E.coli to utilize L-idonate as the sole carbon and energy source. Is also able to catalyze the reverse reaction in vitro, but the D-gluconate oxidation by the enzyme can only proceed with NAD.
P0A9Q0
A5GUP3
COBQ_SYNR3
Cobyric acid synthase
unclassified Synechococcus
MTPPTPLMVLGTSSGAGKSLMTAALCRVLKRRGEQPLPFKGQNMSNNAWVDQSGGEMAYSQALQSWAAGLEPNCAMNPVLLKPQGNSTSEVIHGGESVGMARAETYYQEWFKPGWLAIRQGLEQLRQQHPHGRLVLEGAGSPVEVNLQHRDLTNLRLAQYLRARCLLVADIERGGVFAQLVGTLQLLRPVERPLVKGLLINRFRGRQELFDPGVSWLSDNTGVPVLGVMPWLDELFPPEDSLDLLERRGRKANAELEIAVLRLPSLSNFSDLDPLEAEPSVQLRWVQPGEALGQPDAVVLPGSKQTLRDLKALQASGLARELQRFSAGGGAVLGICGGLQMLGRELLDPDGLEGAAGASAAGLNLLPLQTRFGGSKALRQRQAVAHWPTAESCPIEGFELHRGSTIALEPLQALCQEEGLGWVQGQVAGSYLHGLLENGRWRRQWLNQLRRRKQLPELAEDQGHHSLQREELLDRLADAFEANVDLTPLISDP
Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.
A5GUP3
O08773
RGS14_RAT
Regulator of G-protein signaling 14
Rattus
MPGKPKHLGVPNGRMVLAVSDGELTSTSGSQAQGEGRGSSLSIHSLPSGPSSPFSTDEQPVASWAQSFERLLQDPRGLAYFTEFLKKEFSAENVTFWQACERFQQIPASDTKQLAQEAHNIYHEFLSSQALSPVNIDRQAWLSEEVLAQPRPDMFRAQQLQIFNLMKFDSYARFVKSPLYQECLLAEAEGRPLREPGSSHLGSPDTARKKPKLKPGKSLPLGVEELGQLPLAEGRPLRKSFRREMPGGAVNSALRRESQGSLNSSASLDLGFLAFVSSKSESHRKSLGSGEGESESRPGKYCCVYLPDGTASLALARPGLTIRDMLAGICEKRGLSLPDIKVYLVGKEQKALVLDQDCTVLADQEVRLENRITFQLELVGLERVVRISAKPTKRLQEALQPILAKHGLSLDQVVLHRPGEKQLVDLENLVSSVASQTLVLDTLPDAKTREASSIPPCRSQGCLPRTQTKDSHLPPLSSSLSVEDASGSTGKRQTCDIEGLVELLNRVQSSGAHDQRGLLRKEDLVLPEFLQLPSQRPGSQEAPP
Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Besides, modulates signal transduction via G protein alpha subunits by functioning as a GDP-dissociation inhibitor (GDI) . Has GDI activity on G(i) alpha subunits GNAI1 and GNAI3, but not on GNAI2 and G(o)-alpha subunit GNAO1. Has GAP activity on GNAI0, GNAI2 and GNAI3. May act as a scaffold integrating G protein and Ras/Raf MAPkinase signaling pathways. Inhibits platelet-derived growth factor (PDGF)-stimulated ERK1/ERK2 phosphorylation; a process depending on its interaction with HRAS and that is reversed by G(i) alpha subunit GNAI1. Acts as a positive modulator of microtubule polymerisation and spindle organization through a G(i)-alpha-dependent mechanism. Plays a role in cell division; required for completion of the first mitotic division of the embryo. Involved in visual memory processing capacity; when overexpressed in the V2 secondary visual cortex area. Involved in hippocampal-based learning and memory; acts as a suppressor of synaptic plasticity in CA2 neurons. Required for the nerve growth factor (NGF)-mediated neurite outgrowth. Involved in stress resistance.
O08773
Q32RX2
CYF_STAPU
Cytochrome f
Staurastrum
MQNKDACKSLSSWVSLSISLLVLTVPLIWPYNSTAFPIYAQQNYESPREATGRIVCANCHLAKKAVDIEVPQAVLPDTVFEAVVKIPYDTQIKQVLSNGKKGGLNVGAVLILPEGFELAPSDRIPPELKEKISNIYFQPYSPEKKNILVVGPLPGNKYSELVFPILSPDPATNKKASFLKYPIYLGGNRGRGQVYPDGSKSNNNVFSASTAGTISQITRQKKGGYEVIIKTTDGREVTDIIPPGPELIVSEGESIKADQLLTNNPNVGGFGQADAEIVLQDPLRIQGLLVFFASVILAQIFLVLKKKQFEKVQLAEMNF
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Q32RX2
A9VTA4
FMT_BACMK
Methionyl-tRNA formyltransferase
Bacillus cereus group
MMKVVFMGTPDFSVPVLRRLIEDGYDVVGVVTQPDRPVGRKKVLTPTPVKVEAEKHGIPVVQPLKIREKDEYEKVLALEPDLIVTAAFGQIVPNEILEAPKYGCINVHASLLPELRGGAPIHYAIMEGKEKTGITIMYMVEKLDAGDILTQVEVEIEERETTGSLFDKLSEAGAHLLSKTVPLLIQGKLEPIKQSEAEVTFAYNIKREQEIIDWTKTGEEVYNHIRGLNPWPVAYTTLAGQVIKVWWGEKVSITEKAEPGTIVALEEDGFVVATGNETGVKITELQPSGKKRMSCSQFLRGTKPEIGTKLGENA
Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
A9VTA4
A0RPX5
RS15_CAMFF
30S ribosomal protein S15
Campylobacter
MALDSAKKAEIVAKFARKSGDTGSPEVQVALLTTRISELTGHLKINKKDFSSRLGLLKLVGRRKRLLKYLKAKNYESYTKLIAELGIRDK
Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
A0RPX5
O66914
KDSB_AQUAE
CMP-2-keto-3-deoxyoctulosonic acid synthase
Aquifex
MRRAVIIPARLGSTRLKEKPLKNLLGKPLIRWVVEGLVKTGERVILATDSERVKEVVEDLCEVFLTPSDLPSGSDRVLYVVRDLDVDLIINYQGDEPFVYEEDIKLIFRELEKGERVVTLARKDKEAYERPEDVKVVLDREGYALYFSRSPIPYFRKNDTFYPLKHVGIYGFRKETLMEFGAMPPSKLEQIEGLEQLRLLENGIKIKVLITENYYHGVDTEEDLKIVEEKLKNL
Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
O66914
O13394
CHS5_USTMA
Class-IV chitin synthase 5
Ustilago
MNPFESLPDAARPAQGTRPNRSDGPPPLPPLTIPGSTGRPQNPIFSPPPNLHHILPPGYLPQQQQQQQQQQQQQQQRSQQPFFSPPPPDAMSPPLGSHQAYLNSTSSQPTQRLPGISFQEPQRMPVQRSGPSRDSVKSYGDDKRSINDPNSSSTALTQVNSLDPESGFSAHNDTFRRKKSLVRPDRERMDPSHRQWYYRNHAAHMDVMAASGGRVGYMPSTTGHLPQHGAAPHGSGMAGIVGPGGGLSGLGVTGPTNVPPGGLGRAPPLRRGKSLLGRDEDQVETGINVLKRGVSLRRKQSKSGNKPSKEVPRDLGESKTSRIAPGPVGGWMIYCYILTICCPGPFLRIFGIRTPEQQRAWREKMGLIGIITLIMAAVGFLTFGFTQTVCGQQPDRYTLGTIDVGSMTFNGYDYSFDGFIHPQVGPFGADTIYNRTNPIYSEPWSSGGQDGSLLFQKIGAACTGIISNRAGGAQPERYFDCTLVRQDGKGGYANSTMPMCHTGSIVDQFNDGAQPRNSVLKKRGQVSLQWNNVTDPARNLAVYRGSVLDLNRLNNLTTGLSYPELYDTLKRRNDSWAGRDVTSAVMRQRLEREFQCLEQITRVGFIDSETIGCVASKVELYLSLVFIIGVVAIKFFMAVMFGWFISWRLGNYANETYEQRMKRAAEIEQWSDDIYRPAPAGYRPNARKHKSFLPAKSRFSVADPLSLKSGSRAPMPLSEKRMTRASRLGVASPLGGSPPGSPSVAGGRSSASLAPAHSRRSSFSGSPAEGAMGVCPFPLHNTIPQPGPDYRPFGFQLAHSICLVTAYSESFEGLRTTLDSLATTDYPNSHKLLLVIADGIVKGAGSDISTPDICLSMMKDLVIPAEEVEGNSYVAIADGYKRHNMCKIYAGFYDYDDETVERSKQQRVPMILVAKCGTPLEADSAKPGNRGKRDSQVLLMAFMQKVMFDERMTAFEYEFFNSIWRVTGVSPDNYEIVLCVDADTKVFPDSLSRMVACMVEDPEIMGLCGETKIANKSETWVTMIQVFEYYISHHQTKAFEACFGGVTCLPGCFSAYRIKAPKGPHGYWVPILANPDIVEHYSENVVDTLHKKNLLLLGEDRYLTTLMLKTFPKRKMMFVPQAVCKTIVPDTFRILLSQRRRWINSTVHNLFELVMVNDLCGTFCFSMRFVVFMELTGTLVLPAAIAFTLYVVVQAFLPNVPTPTIPLILLALILGLPGILIVVTSRKIAYVGWMLIYLLSLPIWNFVLPLYAYWHMDDFSWGATRVVQGENKKDNHGDADGKFDPSHIVMKRWAEFERERRWKSGTHSRDSTYDVVQRTGSPERAGSTRYSVVSSDTFHSSPFGQHDQFGRALPNAMSSSSASQFGPDVSEVSHSKSPSGARARLDAVPLLELPAPLATDAKHRSGASPTGTVVVPRPRATSPAPLPHNSGHPALGSVSAFSPTQHSAGRLPTLPGAATYEAYPHTDAADEERRPMIGSTSSSPDPEPRRYIGPDAGVRHGNVSTEQRYPTVSESAYPMQAYTAEPETDGSASPTPAQQGFNAANSNQQTRPLTRGFSLVDDGPVASAQGVRQVQRGARRSQMPNSAASPPPANRTGNLPPGAAPPSFD
Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
O13394
Q49YA5
ENGB_STAS1
Probable GTP-binding protein EngB
Staphylococcus
MKVNPNEIELLISAVKPEQYPETGLSEVGLSGRSNVGKSTFINSMIGRKNMARTSQQPGKTQTLNFYNIDNQLVFVDVPGYGYAKVSKKQREAFGKMIEKYISQREELKLVIQLVDLRHNPTEDDILMYNYLKYYEIPTFVVATKEDKIAKGKVQKHLANIQQKLEMEPEDEIISYSSVKNNKQQQIWNVIEKYL
Necessary for normal cell division and for the maintenance of normal septation.
Q49YA5
Q11QB5
RL2_CYTH3
50S ribosomal protein L2
Cytophaga
MSLKKFRPITPGTRFRVAASYDDVTTSTPEKSLVVSIKKSGGRNSQGKMTMRYIGGGHKQQYRIIDFKRDKHAIPAVVKTIEYDPNRTARIALLSYADGEKRYIIAPTGLEVGNTILSGPGIAPEVGNCLPLSDIPLGTVVHNIELKPGKGAAMARSAGTYAQLVAREGKYATLKLPSGEMRMVLVVCYASIGTVSNADHMNLTKGKAGATRWAGRRPRVRGVAMNPVDHPMGGGEGRSSGGHPRSRKGLYAKGGKTRSANKYSKNMIVKKRVNKRLSK
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome.
Q11QB5
Q11UV2
TRMB_CYTH3
tRNA(m7G46)-methyltransferase
Cytophaga
MARKKLMRFKWNEEVHNLFQPEKENYKAYKGKWHEYFKNDNPVILEVGCGRAEYTTGLAALFPENNYIGLDIKGARLWKGSSLSIETGLTNTAFIRTKLQNLEEFFEPGEVKGIWITFPDPKPRESEAKLRLSGLRFMNIYRRLMPAGGKVFFKTDNRVLFDHTLEVLTDQTLKIKDLVFTHDLYQSPLLAEHYGIQTTYEKTYLNQGVQINYLKFEFLPL
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Q11UV2
B2UEL8
RL4_RALPJ
50S ribosomal protein L4
Ralstonia
MELKLLQDNGQLGAGVAASPEVFGRDYNEALVHQVVVAYQANARSGNRKQKDREEVKHTTKKPWRQKGTGRARAGMSSSPLWRGGGRIFPNSPEENFSQKVNKKMYRAGMRSIYSQLAREGRINVVDSLSVDAPKTKLLADKFRAMGLDSVLVITDNLDENLFLASRNLAHVLVVEPRHADPLSLVHYKKVLVTKAAVAQIEELLK
Forms part of the polypeptide exit tunnel.
B2UEL8
Q6P087
RUSD3_HUMAN
RNA pseudouridylate synthase domain-containing protein 3
Homo
MRAVLAREMDGRRVLGRFWSGWRRGLGVRPVPEDAGFGTEARHQRQPRGSCQRSGPLGDQPFAGLLPKNLSREELVDALRAAVVDRKGPLVTLNKPQGLPVTGKPGELTLFSVLPELSQSLGLREQELQVVRASGKESSGLVLLSSCPQTASRLQKYFTHARRAQRPTATYCAVTDGIPAASEGKIQAALKLEHIDGVNLTVPVKAPSRKDILEGVKKTLSHFRVVATGSGCALVQLQPLTVFSSQLQVHMVLQLCPVLGDHMYSARVGTVLGQRFLLPAENNKPQRQVLDEALLRRLHLTPSQAAQLPLHLHLHRLLLPGTRARDTPVELLAPLPPYFSRTLQCLGLRLQ
Catalyzes uridine to pseudouridine isomerization (pseudouridylation) of specific mitochondrial mRNAs (mt-mRNAs), a post-transcriptional modification necessary for their translation. Acts at position 390 in COXI mt-mRNA and at position 697-699 in mitochondrial COXIII mt-mRNA . As a component of a functional protein-RNA module, consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mitochondrial ribosomal RNA (16S mt-rRNA), controls 16S mt-rRNA abundance and may play a role in mitochondrial ribosome biogenesis .
Q6P087
O46107
LIP1_DROME
Lipase 1
Sophophora
MRCSLRMQLLLLLGLCVFISRIQGQLIGGEEDEEDEEEEEEEEESVEDETPEDRLQRKNIKQDSTLSVDKLIAKYGYESEVHHVTTEDGYILTMHRIRKQGAPPFLLQHGLVDSSAGFVVMGPNVSLAYLLADHNYDVWLGNARGNRYSRNHTTLDPDESKFWDFSWHEIGMYDLPAMIDHVLKVTGFPKLHYAGHSQGCTSFFVMCSMRPAYNDKVVSMQALAPAVYAKETEDHPYIRAISLYFNSLVGSSIREMFNGEFRFLCRMTEETERLCIEAVFGIVGRNWNEFNRKMFPVILGHYPAGVAAKQVKHFIQIIKSGRFAPYSYSSNKNMQLYRDHLPPRYNLSLVTVPTFVYYSTNDLLCHPKDVESMCDDLGNVTGKYLVPQKEFNHMDFLWAIDVRKMLYRRMLQVLGKVPEGSPEEANRSRREIRGKFIRS
Could be a digestive enzyme.
O46107
P48031
GBX2_MOUSE
Stimulated by retinoic acid gene 7 protein
Mus
MSAAFPPSLMMMQRPLGSSTAFSIDSLIGSPPQPSPGHFVYTGYPMFMPYRPVVLPPPPPPPPALPQAALQPALPPAHPHHQIPSLPTGFCSSLAQGMALTSTLMATLPGGFSASPQHQEAAAARKFAPQPLPGGGNFDKAEALQADAEDGKAFLAKEGSLLAFSAAEAVQASLVGAVRGQGKDESKVEDDPKGKEESFSLESDVDYSSDDNLPGQTAHKEEDPGHALEETPQSGGAAGSTTSTGKNRRRRTAFTSEQLLELEKEFHCKKYLSLTERSQIAHALKLSEVQVKIWFQNRRAKWKRVKAGNANSKTGEPSRNPKIVVPIPVHVSRFAIRSQHQQLEQARP
May act as a transcription factor for cell pluripotency and differentiation in the embryo.
P48031
A8L568
LEUD_FRASN
Isopropylmalate isomerase
null
MEAFTIHTGRAVPLRRSDVDTDQIIPSEWLKRIERTGFGAGLFSEWRADPSFVLNDPAHAGASILLAGPDFGTGSSREHAVWALQDYGFRAVLSPRFADIFRGNALGNGLLPVVLPADTVEALTAAVEADPTTEITVDLVAREVRGAGQVAGFELDDFTRWRLMEGLDDVGLTLRHEQDITVFEASRPGWLPTTA
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
A8L568
Q057D8
KAD_BUCCC
Adenylate monophosphate kinase
Buchnera
MRIIMIGPPGSGKGTQTQLLSKYFHIPCISTGEILRKEIKKNKKTKKYIKKTINKGKLIKNSFIIKIIEKNIKKKKFFNGFILDGFPRNIEQAKSLSKKINIEYIIYLKIKYDDIIKRITGRLIHASSGRTYHKIFNPPKIKNKDDITQEKLCSRNDDNEKTIKIRLQEYKKHTNPLIKWIKKKKKIKFIEIHANQSIKIVNKKIIYNINNNNINK
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Q057D8
B7MY64
DNLJ_ECO81
Polydeoxyribonucleotide synthase [NAD(+)]
Escherichia
MESIEQQLTELRTTLRHHEYLYHVMDAPEIPDAEYDRLMRELRELETKHPELITPDSPTQRVGAAPLAAFSQIRHEVPMLSLDNVFDEESFLAFNKRVQDRLKSNEKVTWCCELKLDGLAVSILYENGVLVSAATRGDGTTGEDITSNVRTIRAIPLKLHGENIPARLEVRGEVFLPQAGFEKINEDARRTGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGVLEGGELPDTHLGRLMQFKAWGLPVSDRVTLCESAEEVLAFYHEVEKDRPTLGFDIDGVVIKVNSLAQQEQLGFVARAPRWAVAFKFPAQEQMTFVRDVEFQVGRTGAITPVARLEPVHVAGVLVSNATLHNADEIERLGLRIGDKVVIRRAGDVIPQVVNVVLSERPEDTREVVFPTHCPVCGSDVERVEGEAVARCTGGLICGAQRKESLKHFVSRRAMDVDGMGDKIIDQLVEKEYVHTPADLFKLTAGKLTGLERMGLKSAQNVVNALEKAKETTFARFLYALGIREVGEATAAGLAAYFGTLEALEAASIEELQKVPDVGIVVASHVHNFFAEESNRNVISELLAEGVHWPEPIVINAEEIDSPFAGKTVVLTGSLSQMSRDDAKARLVELGAKVAGSVSKKTDLVIAGEAAGSKLAKAQELGIEVIDETEMLRLLGS
DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
B7MY64
Q88UX4
THII_LACPL
tRNA 4-thiouridine synthase
Lactiplantibacillus
MQYTEIMVRYGELSTKGKNRRNFIDSLGRNVRKALHDFPELKVHANRDRMHIMLNGEDADKVMGRLKLVFGIQNFSPSIRVDADMDAVYETAIAMVKAQFKPGMTFKIYTRRSDHQFEYDTNQINDMLGGQILDHVDGIQVKMKNPDIVLRVEVRLNGIFLSSETIQGAGGLPVGTAGKGMLMLSGGIDSPVAGYLGMKRGVDMEMVHFFSPPYTSEQALAKAKQLASTLASYSGSVKFIQIPFTEIQEEIKEKVPEGYLMTVQRRLMMRLMDAITRQRHGKAIFNGESLGQVASQTMDSMIAINDVTTLPVLRPVISMDKTEIIKIAEDIDTYDLSIMPFEDCCTIFAPPAPKTHPKLDRSRSYEERIDVEGLMARALAGVKMTEIKPGENYLNTQEDVFAELL
Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
Q88UX4
Q1R0G4
RL24_CHRSD
50S ribosomal protein L24
Chromohalobacter
MRKIKRDDEVIVIAGKDKGKRGTIKRVLQDGCYVVSGVNMIKRHTKPNPMQGKQGGIVEREAPIHASNVAIFNQETGKADRVGFQIQEDGTKVRIYKSTQKQIDA
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
Q1R0G4
P20044
REPA_LACPN
Protein RepA
Lactiplantibacillus
MVEVEKKKITLSIPVETNGKLEELAQKYGMTKSGLVNFLVNQVAEAGTIYRQ
Regulates the plasmid copy number. RepA binds to the repAB promoter thus controlling the synthesis of the plasmid replication initiator protein RepB.
P20044
Q8NG35
D105A_HUMAN
Defensin, beta 105
Homo
MALIRKTFYFLFAMFFILVQLPSGCQAGLDFSQPFPSGEFAVCESCKLGRGKCRKECLENEKPDGNCRLNFLCCRQRI
Has antibacterial activity.
Q8NG35
Q1GZB8
RSMA_METFK
S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase
Methylobacillus
MKHVAKKRFGQNFLTDRAIINSLIDAIAPQPQDCMVEIGPGLGAMTQPLLERLQHLHVVEIDRDIIQWMQGHYPQDKLTIYASDALKFNFGNISDRLRVVGNLPYNISTPILFHLLDNVPHIIDMHFMLQKEVVERMVAAPSSAAYGRLSVMLQYRLHMEYLLTVPPEAFDPAPKVESAFVRAVPYTVLPHPAKDEALLGRIVTAAFAQRRKTLRNTLKGLLDDTGFASLGIDPQLRAENIAPAGFVAIANYLAA
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.
Q1GZB8
Q1ISS4
GPMI_KORVE
2,3-bisphosphoglycerate-independent phosphoglycerate mutase
Candidatus Koribacter
MPTPKPLVLIILDGWGYAPPSNANAISLARKPNYDKLLTDFPNTLIHTSGRYVGLPPGQMGNSEVGHLNIGAGRVVYMDITKIDLAIENKSLFKNQTLLDAMKHAANGRQLHFFGLLSDGGVHSHQNHLYALLRMAKENGVERVFVHPFMDGRDTLPTNGVKYVDQLQQKMREYGIGKIASISGRYYAMDRDKKWDREKLASDAMLHGRGEGGRYKDPVQGIKESYNKGVTDEFIIPFVCVDDNDQPIGVIRDGDACINFNFRADRARQITRVLARNSGITKDGGRELDAADTLDATIPRDTIPKDLHYTCMTQYDPKFTLPIVIPPDTLTHILANEMAAMNMRNLRVAETEKYAHVTYFFNGGIEKPYPGEERELVQSPKVATYDLKPEMSANGIADVIEHAVEKGAFDVIVVNFANADMVGHSGKIPPTITAVETVDSCLGRVYNVVRKKGGAMLITADHGNAEQMIDPETGGPQTAHTTNPVPFIFVAEDAKKRFSLRPDGALQDISPTMMGILGIPQPKEMTGHDLRVDLTVKK
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Q1ISS4
P55963
CA4A_CONPU
Alpha-A-conotoxin PIVA
Chelyconus
MFTVFLLVVLATTVVSFTSDRASDDRNTNDKASRLLSHVVRGCCGSYPNAACHPCSCKDRPSYCGQGR
Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin has higher affinity for the adult subtype (alpha-1/beta-1/gamma/delta subunits) (IC(50)=2.3 nM) of the receptor than for the fetal subtype (alpha-1/beta-1/epsilon/delta subunits) (IC(50)=22 nM).
P55963
A3MNU6
SYDND_BURM7
Non-discriminating aspartyl-tRNA synthetase
pseudomallei group
MSMRTEYCGLVTEHLLGQTVSLCGWVHRRRDHGGVIFIDLRDREGLVQVVCDPDRAEMFAAAEGVRNEFCIQVKGLVRGRPEGTINAGLKSGRIEVLCHELNVLNASVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQHNLRLRYRVAIEARKYLDEQGFIDIETPMLTKSTPEGARDYLVPSRVNAGQFFALPQSPQLFKQLLMVANFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLGEQEIRDLFEDMIRHIFKTTIGVELDATFPVMPYSEAMARFGSDKPDLRVKLEFTELTDAMKDVDFKVFSTPANTKDGRVAALRVPKGGELTRGDIDGYTEFVRIYGAKGLAWIKVNERAKGRDGLQSPIVKNLHDASIAAILERTGAQDGDIIFFAADRAKVVNDSLGALRLKIGHSEFGKANGLVEAGWKPLWVVDFPMFEYDDEEARYVAAHHPFTSPKDEHLEYLETDPGRCLAKAYDMVLNGWEIGGGSVRIHREEVQSKVFRALKIGPEEAQAKFGFLLDALQYGAPPHGGIAFGLDRIVTMMAGADSIRDVIAFPKTQRAQCLLTQAPSPVDERQLRELHIRLRQPEQPKA
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
A3MNU6
Q9YCQ6
GLMS_AERPE
L-glutamine--D-fructose-6-phosphate amidotransferase
Aeropyrum
MCGIIGLAFAEGNSVAGALVRGLKRLEYRGYDSMGVAVIEPPGRLVVRKAAGKIGEVVRRTGVLSLRGRVGIGHTRWATHGPPNDVNAHPHTDCGGRVAVVHNGVIRNYASLRRELEARGHRLVSETDTELVAHLIEEYLGRGYSFLEALSLLGRVLRGSYALALLHLGEPDKVYFLRYKSPLVVGLGEGVNAVASDITAVLDVARDVIVLEDGEFGWISPEGVAIYRPRGDGGFEPLPPGALEERVKRVEWTPESASKAGYPHFMLKEIYEQPRALAETFEGIIEDPALLRAAGLVAGAGRLLIVGAGTSFHAGLVGHYYLSRLAGILGHPVVASEHKVYTPGVDGETVVVAVSQSGETYDTLEAVREWRGRGARVIGVTNVVGSALDREADVTLYLRAGPEIGVAATKTFLAQTILLQTLSIAAAGEAGRLTSGETRELTGVLEGAPDAARRAILASEGAAREAASLLKGAGSMYIIGRGLGGRLAMEAALKVKEVSYIHAEAYPAGESKHGPIALVEPGFKVYVVATSDSPEVMGNAIEMKARGASVTVVAPSDLQLDTPEGIEVLKMPPTGGETLLDPYSLTPYFQLLAYHLAVARGYDPDKPRNLAKTVTVE
Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Q9YCQ6
O04986
HBL1_ORYSJ
rHb1
Oryza sativa
MALVEDNNAVAVSFSEEQEALVLKSWAILKKDSANIALRFFLKIFEVAPSASQMFSFLRNSDVPLEKNPKLKTHAMSVFVMTCEAAAQLRKAGKVTVRDTTLKRLGATHLKYGVGDAHFEVVKFALLDTIKEEVPADMWSPAMKSAWSEAYDHLVAAIKQEMKPAE
May not function as an oxygen storage or transport protein, but might act as an oxygen sensor or play a role in electron transfer, possibly to a bound oxygen molecule. Has an unusually high affinity for O(2) because of a very low dissociation constant.
O04986