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
|
|---|---|---|---|---|---|---|
A9NBA8
|
MNMG_COXBR
|
Glucose-inhibited division protein A
|
Coxiella
|
MQSTSQQFDVIVVGGGHAGTEAALVAARMGARTLLLTHNIETLGQMSCNPAIGGIGKSHLVKEIDALGGIMALAADQAGIHFRTLNARKGPAVRATRAQADRVLYKAAIHHALENQPHLWLFQQGVDDLIIQNNRAAGVVTQMGLAFYAPTVILTVGTFLGGKIHIGMNHYRGGRAGDPPALALAERLREMPFRVERLKTGTPPRIDGRTINYSQLIEQPSDQPLPLMSYWSHGEDRPRQVSCFITQTNEKTHDIIRNGLKTSPLFSGVIEGVGPRYCPSIEDKIVRFADRNSHQLFLEPEGLNTPEVYPNGVSTSLSFDVQLDFIHSIKGLEKCHITRPGYAIEYDYFDPRDLKPSLETKYVPGLYFAGQINGTTGYEEAAAQGLIAGINAALQIQERAPWTPARDEAYIGVLIDDLTTRGTNEPYRMFTSRAEYRLLLRQDNADLRLTEKGRDLGCVDDERWNFFVKKKETIEKEQQRLKKQRIWPKSTVAKAIESRFQQLLERDYSAMDLLRRPEINYPALMQIEELGPAVLEPSVAEQIDIQAKYEGYLTHQLAEIARQKKYQTAQIPSSLDYNQVTGLSNEVRQKLNETKPTTLGQASRIPGITPAAISLLLVHLKKKELYP
|
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.
|
A9NBA8
|
C6DE12
|
RL9_PECCP
|
50S ribosomal protein L9
|
Pectobacterium
|
MQVILLDKVANLGSLGDQVNVKAGYARNFLVPQGKAVPATKKNVEFFEARRAELEAKLADVLAAAEARAAKIKELGSVTIASKAGDEGKLFGSIGTRDIADAVTAAGVDIAKSEVRLPNGVLRTLGEHEVSFQVHSDVFAELNVVVVAEA
|
Binds to the 23S rRNA.
|
C6DE12
|
P21126
|
UBL4A_MOUSE
|
Ubiquitin-like protein GDX
|
Mus
|
MQLTVKALQGRECSLQVAEDELVSTLKHLVSDKLNVPVRQQRLLFKGKALADEKRLSDYNIGPNSKLNLVVKPLEKVLLEEGSAHRLVDSPATPIWQLISKVLARHFSVADASRVLEQLQRDYDRSLSRLTLDDIERLASRFLHPEVTEAMEKGFCK
|
As part of a cytosolic protein quality control complex, the BAG6/BAT3 complex, maintains misfolded and hydrophobic patches-containing proteins in a soluble state and participates in their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation. The BAG6/BAT3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endoplasmic reticulum membrane. Recruited to ribosomes, it interacts with the transmembrane region of newly synthesized tail-anchored proteins and together with SGTA and ASNA1 mediates their delivery to the endoplasmic reticulum. Client proteins that cannot be properly delivered to the endoplasmic reticulum are ubiquitinated and sorted to the proteasome. Similarly, the BAG6/BAT3 complex also functions as a sorting platform for proteins of the secretory pathway that are mislocalized to the cytosol either delivering them to the proteasome for degradation or to the endoplasmic reticulum. The BAG6/BAT3 complex also plays a role in the endoplasmic reticulum-associated degradation (ERAD), a quality control mechanism that eliminates unwanted proteins of the endoplasmic reticulum through their retrotranslocation to the cytosol and their targeting to the proteasome. It maintains these retrotranslocated proteins in an unfolded yet soluble state condition in the cytosol to ensure their proper delivery to the proteasome.
|
P21126
|
Q9FPH0
|
XB34_ARATH
|
RING-type E3 ubiquitin transferase XBAT34
|
Arabidopsis
|
MGQQQSQSKDEMLFQEVSNNNVEGIKSLHHEGAGLEGVDKLGRTPLILACTNDDLYDVAKTLLELGSNVNAYRSGCNGGTPLHHAAKRGLVHTVKLLLSHGANPLVLDDDVKTALEVARDEGYSNVVRAIESHICLFSGCMREYSGSSLLNLFAPQLLSRKVWVVVVPTGSRNPTKPLKLELVLYDSIQDAQPRMVIPLWKANLEEPKSFRCDDSVMIIDDSRSPKSMRQRRESGFISQARRWAQVDRQIRLKLAAEIKGDMKQMNWFSEACKGVPQPMNPPRFMKTSQATTTTTNVPALSDDALTRVAMSLPSPKTANKEDGLCVICVDAPSEAVCVPCGHVAGCISCLKEIENKKMGCPVCRANIDQVIKLYHV
|
No E3 ubiquitin-protein ligase activity observed when associated with the E2 enzyme UBC8 in vitro.
|
Q9FPH0
|
Q126P9
|
KYNB_POLSJ
|
N-formylkynurenine formamidase
|
unclassified Polaromonas
|
MTARVLPSTTAKPLRLWDISPPVAPGSPVFPGDTPYQQQWAASIAPGCPVNVSTLTLSPHIGAHADAPLHYDPQGATIGAVDLTPYIGPCRVIHAIAKGPLIEWEHLAHAVHDLPPRVLVRTYARMPVERWDPTLAAYAPETVERLAALGVKLIGIDTASIDPAGSKTLDSHQVIRQRGLRVLENLVLDEVPEGDYELIALPLKLMTADASPVRAVLRELP
|
Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation.
|
Q126P9
|
Q54JR9
|
ECD_DICDI
|
Protein ecdysoneless homolog
|
Dictyostelium
|
MNKAKNSGAVPQFVDNFEDFYNNGDDILNNKHKEEINFVKYRIFDTHLINYNNNNNNKNNNNNNNNNENTTITNKLNEIKEYLILNYIKDYIWQKEPFNLKIYDHKKKQQQQQQLPIHFYGNTKFEESIDDEWFIVYILLELTKKFQSLIVSIKDNDGEFILIETAQALPKWIKPTNSNNRVYLKNGEIHIIPLPSDPSQLDTIPYKMDTNTALSILSSSSNNIITKVSNEINEILKNRLKRFYNGEYFLKDQNQIKLAAIPIEIGYLLNQYPQLISDITTTFYNRDSDDMKTISTMKRFPMSRERDSFGNSGQLITTNIRFTRCLYAMLKLQQWNSPKNFHPQLPKPSHPTYDSRSLGVKIICGLEMVYNRSKRNSVSSYHRFNDDLNWLNYLKQLKSNNYFNDETIGSKLYKEKLLIAKNQYLKNNINNNNNNNNKEEESIYKLIDQVTNSKSVDEMIKILQESDKSKIESEDDWLNEENPDKFEDLITEFENDRQKQQQKQQQQQQQQQQNKEGKKEVKENNNNNNNNNNNNNNNNNNNNNNNNNNNNDSNLINDFSNQFKSMLSQLSSFDGVEFNEKSGNSKNKTKSSAYGNGGDDNISFDSNKFMDILKGFTDNNKYDDDYDDDDDDDDDMYQDIDNYEDSDDKDDDEDDENDEDDEDDGFEEYEDEDEDDDDEKEFQYVEFLKKSTIKQYMERMDQELNLKIIASSFELESTKLPKEFDDIEKSNNNNNNNINNNDKDVDEDDNENYKVNQKVDLNLNLVKNLLESLTEQQGFAGPASTLLKEMSDNNSKKREKKKTSSKKLIPKKGKVKENK
|
May act as a transcriptional activator.
|
Q54JR9
|
Q74IC4
|
IF3_LACJO
|
Translation initiation factor IF-3
|
Lactobacillus
|
MILNEDIRAREVRLIGVDGQQVGVVSKNEALRKAADADLDLVLLSPNAKPPVARIMDYGKFRFEQQKKAKENRKNQKVMAVKEIRLSPTIEGNDFDTKLKHVRKFLTKGAKVRVSIRFRGRAITHKELGKQVLEKMADEASDLSNVVTKPKMEGRSMFLMLAPLSEKDKKKK
|
IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins.
|
Q74IC4
|
P0AES8
|
GYRB_SHIFL
|
DNA gyrase subunit B
|
Shigella
|
MSNSYDSSSIKVLKGLDAVRKRPGMYIGDTDDGTGLHHMVFEVVDNAIDEALAGHCKEIIVTIHADNSVSVQDDGRGIPTGIHPEEGVSAAEVIMTVLHAGGKFDDNSYKVSGGLHGVGVSVVNALSQKLELVIQREGKIHRQIYEHGVPQAPLAVTGETEKTGTMVRFWPSLETFTNVTEFEYEILAKRLRELSFLNSGVSIRLRDKRDGKEDHFHYEGGIKAFVEYLNKNKTPIHPNIFYFSTEKDGIGVEVALQWNDGFQENIYCFTNNIPQRDGGTHLAGFRAAMTRTLNAYMDKEGYSKKAKVSATGDDAREGLIAVVSVKVPDPKFSSQTKDKLVSSEVKSAVEQQMNELLAEYLLENPTDAKIVVGKIIDAARAREAARRAREMTRRKGALDLAGLPGKLADCQERDPALSELYLVEGDSAGGSAKQGRNRKNQAILPLKGKILNVEKARFDKMLSSQEVATLITALGCGIGRDEYNPDKLRYHSIIIMTDADVDGSHIRTLLLTFFYRQMPEIVERGHVYIAQPPLYKVKKGKQEQYIKDDEAMDQYQISIALDGATLHTNASAPALAGEALEKLVSEYNATQKMINRMERRYPKAMLKELIYQPTLTEADLSDEQTVTRWVNALVSELNDKEQHGSQWKFDVHTNAEQNLFEPIVRVRTHGVDTDYPLDHEFITGGEYRRICTLGEKLRGLLEEDAFIERGERRQPVASFEQALDWLVKESRRGLSIQRYKGLGEMNPEQLWETTMDPESRRMLRVTVKDAIAADQLFTTLMGDAVEPRRAFIEENALKAANIDI
|
A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
|
P0AES8
|
Q9X5V1
|
AHPD_STRVD
|
Alkylhydroperoxidase AhpD
|
Streptomyces
|
MSLDSLKSRIPDYAKDLKLNLGSVIGNSGLPAQQLWGTVLSTAIASRSAIVLRELEPEAKANLSPEAYTAAKAAAAVMAMNNVFYRTRHLLSDHEYGNLRAGLRMNVIGNPGVDKVDFEFWSFAVSAINGCGMCLDSTKQVLRKAGVERRSSRRRSDCRGTQAVAATLDAEAFS
|
Antioxidant protein with alkyl hydroperoxidase activity. Required for the reduction of the AhpC active site cysteine residues and for the regeneration of the AhpC enzyme activity.
|
Q9X5V1
|
Q3ZYS0
|
MIAB_DEHMC
|
tRNA-i(6)A37 methylthiotransferase
|
Dehalococcoides
|
MPGYYLWTIGCQMNQAESDRLGRLFELWGYSLADKAEDAELVLVNSCVVREHAENKVVNRLHLLRSLKNKNPKLKIALTGCLVGQDISLIKKKFPFVDYIFGPGSMPDWREIPEGFILPLRPPVSANVTIMQGCNNFCTYCVVPYRRGREKSRSIAEIGCEVAELVRRGSREVVLLGQNVDSYGHDLPEKPCLADLLSALHDITGLLRIRFLTSHPKDISQKLIDAMAHLPKVCRSLSLPVQSGDDTILASMRRGYTNQQYRELVERIKTAMPDISLQTDLIVGFPSENEEQFNQSYKLMADIGYDAIHVAAYSPRPQTVAARDMADDVPVIEKKRRLKLIEDLQKETVGKANAALMDTFAEVLVEGLQKNKWQGRTLGGKLVFLESDLPLEGCLVKVKIFKTSPWSLQAKLVNILES
|
Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
|
Q3ZYS0
|
Q9LJB7
|
BBX32_ARATH
|
EIP6, EMF1-INTERACTING PROTEIN 6
|
Arabidopsis
|
MVSFCELCGAEADLHCAADSAFLCRSCDAKFHASNFLFARHFRRVICPNCKSLTQNFVSGPLLPWPPRTTCCSESSSSSCCSSLDCVSSSELSSTTRDVNRARGRENRVNAKAVAVTVADGIFVNWCGKLGLNRDLTNAVVSYASLALAVETRPRATKRVFLAAAFWFGVKNTTTWQNLKKVEDVTGVSAGMIRAVESKLARAMTQQLRRWRVDSEEGWAENDNV
|
Repressor of light-mediated regulation of seedling development. Functions by suppressing the activities of positive cofactors like BBX21 and HY5 involved in modulating light-regulated gene expression and growth.
|
Q9LJB7
|
Q4AAR4
|
DNAK_MESHJ
|
Heat shock protein 70
|
Mesomycoplasma
|
MAKEIILGIDLGTTNSVVAIIENQKPVVLENPNGKTTTPSVVAFKNNEEIVGDAAKRQLETNPEAIASIKRLMGTDKTVRANERDYKPEEISAKILAYLKEYAEKKIGHKVTKAVITVPAYFDNAQREATKNAGKIAGLQVERIINEPTAAALAFGLDKTEKEMKVLVYDLGGGTFDVSVLELSGGTFEVLSTSGDNHLGGDDWDNEIVNWLVKKIKEEYDFDPKSDKMALTRLKEEAEKTKINLSNQSVSTVSLPFLGMGKNGPINVELELKRSEFEKMTAHLIDRTRKPIVDALKQAKIEASDLDEVLLVGGSTRMPAVQSMIEHTLNKKPNRSINPDEVVAIGAAIQGGVLAGEISDVLLLDVTPLTLGIETLGGIATPLIPRNTTIPVTKSQIFSTAEDNQTEVTISVVQGERQLAADNKMLGRFNLSGIEAAPRGLPQIEVSFSIDVNGITTVSAKDKKTGKEQTITIKNTSTLSEEEINKMIQEAEENREADALKKDKIETTVRAEGLINQLEKSITDQGEKIDPKQKELLEKQIQELKDLLKEEKTDELKLKLDQIEAAAQSFAQATAQQANTSESDPKADDSNTIDAEIKQD
|
Acts as a chaperone.
|
Q4AAR4
|
A0A0C4DH42
|
HV366_HUMAN
|
Immunoglobulin heavy variable 3-66
| null |
MEFGLSWVFLVAILKGVQCEVQLVESGGGLIQPGGSLRLSCAASGFTVSSNYMSWVRQAPGKGLEWVSVIYSCGSTYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAR
|
V region of the variable domain of immunoglobulin heavy chains that participates in the antigen recognition . Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens . The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen .
|
A0A0C4DH42
|
B3F211
|
IBP2B_DANRE
|
Insulin-like growth factor-binding protein 2-B
|
Danio
|
MSLALLCSLLLVHGSLGEIVFRCPSCTAERQAACPKLTTSCEIVREPGCGCCPVCARQKGELCGVYTTRCGSGLRCYPSANSELPLEQLIQGLGRCENKVDLEPTMTNQESAAHSGEVNGTRSPPMKKPGKDYQYIKEIAVNKHHNNKRTRMYNTQDDPKTPHPKQSQCQQELDKVLENISRMAFHDNKGPLENLYDLKFPNCDKTGQYNLKQCHMSTHGQRGECWCVNPYTGVQIPSSDKVRGDPNCSQYYGGPELEPPTAQQK
|
IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors.
|
B3F211
|
B5FBH8
|
RLMG_ALIFM
|
rRNA (guanine-N(2)-)-methyltransferase RlmG
|
Aliivibrio
|
MKTELSLLDRSLNLQRYPKRAQELLQAWDAGDEYIIKYVEEELNLEDGKNILILNDNFGALSCWFSDKHNVTMMTDSFVSQRGTLKNLQRNQCNRVQLITSTEEMPQGFDLVLMQIPKNNRMLTWQLQQLRQSMDSSCPIIAVNKAKEIHSSTLELFEDYLGETKTSLAWKKHRLVFSNANASNPKTIAEAVCWSVDNEDIDLLNYPNVYSGEKLDQGARFMLEHIPSDPELRHIIDLGCGNGVLSVKAGQLNPEARITCVDESFMAVESARRNLEVNLGKERQFQFIANNCLDGFKKHSSYLVLCNPPFHQGQAITDHIAWQMFCDAKHILCKDGKLLVIGNRHLDYDGKLCRLFGEENVTTVASNSKFVILEAVKAEKSK
|
Specifically methylates the guanine in position 1835 (m2G1835) of 23S rRNA.
|
B5FBH8
|
Q724E9
|
RPOC_LISMF
|
Transcriptase subunit beta'
|
Listeria
|
MLDVNNFEYMKIGLASPDKIRSWSHGEVKKPETINYRTLKPERDGLFCERIFGPMKDWECSCGKYKRVRYKGVVCDRCGVEVTKSKVRRERMGHIELAAPVSHIWYFKGIPSRMGLVMDMSPRALEEIIYFASYVVTEPGDTPLEKKQLLSEREYRVYREKYGKGFSAGMGAEAIKKILADIDLEKETNDLKEELKSAQGQRRTRAIRRLEVMEAFRNSGNNPSWMVLDVLPVIPPEIRPMVQLEGGRFATSDLNDLYRRVINRNNRLKRLLDLGAPNIIVQNEKRMLQEAVDALIDNGRRGRPVTGPGNRPLKSLSHMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPNLKMYQCGLPKEMALELFKPFVMKELVGRGLAHNIKSAKRKIERMAPEIWDVLEEVIREHPVLLNRAPTLHRLGIQAFEPTLVEGRAIRLHPLVCTAYNADFDGDQMAVHVPLSAEAQAEARILMLAAQNILNPKDGKPVVTPSQDMVLGNYYLTLERENAVGEGTIFKDINEAQLAYQNGYVHLHSRIAVFAGSIPNERFTDEQRNQLLITTVGKLIFNTILPKSFPYINEPTKFNLEIETPAKYFVDTTTDVRAHIAAQELIDPFKKKILGNIIAEVFKKFHITETSKMLDRMKDLGFKISTKAGMTVGIADILTLEEKHEILEKAHDTVEKITKSFRRGLITDDERYERVIGVWNAAKDEIQGKLILSLDRLNPIFMMQDSGARGNISNFTQLAGMRGLMADPSGRIVELPITSNFREGLTVLEYFISTHGARKGLTDTALKTADSGYLTRRLVDVAQDVIIREDDCGTDRGLTIKAIREGTEIIEPLEERLEGRYSRKTIRHPETKEVIARENDLITEAIATQIVDAGIEEVTIRSAFTCNTKHGVCKKCYGKNLATGTEVEVGEAVGIIAAQSIGEPGTQLTMRTFHTGGVAGDDITQGLPRIQEIFEARNPKGQAIITEVGGEVVSIEEGRDRQQEITIQGTDDRRSYNIPYTARLRVEEGTIVERGEALTEGSVDPKALIRVRDVLSVQEYLLAEVQKVYRMQGVEIGDKHVEVMVRQMLRKIRVMDTGDTNILPGTLMDIHTFTEANRDAILSGSQPATGRPVLLGITKASLETDSFLSAASFQETTRVLTDAAIKGKRDELLGLKENVILGKLVPAGTGIGRYRKLKSEVIKETAEVTDEITNI
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
Q724E9
|
B1LLL8
|
MENH_ECOSM
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase
|
Escherichia
|
MILHAQAKHGKPGLPWLVFLHGFSGDCHEWQEVGEVFADYSRLYVDLPGHGGSAAISVDGFDDVTGLLCKTLVSYNILDFWLVGYSLGGRVAMMAACQGLAGLCGVVVEGGHPGLQNAEQRTQRQRSDRQWAQRFRTEPLTAVFADWYQQPVFASLNDEQRRELVALRSNNNGATLAAMLEATSLAVQPDLRANLSARTFAFYYLCGERDSKFRALAAELAAECHVIPRAGHNAHRENPAGVIASLAQILRF
|
Catalyzes a proton abstraction reaction that results in 2,5-elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC) and the formation of 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC).
|
B1LLL8
|
P66814
|
NPD_MYCBO
|
Regulatory protein SIR2 homolog
|
Mycobacterium tuberculosis complex
|
MRVAVLSGAGISAESGVPTFRDDKNGLWARFDPYELSSTQGWLRNPERVWGWYLWRHYLVANVEPNDGHRAIAAWQDHAEVSVITQNVDDLHERAGSGAVHHLHGSLFEFRCARCGVPYTDALPEMPEPAIEVEPPVCDCGGLIRPDIVWFGEPLPEEPWRSAVEATGSADVMVVVGTSAIVYPAAGLPDLALARGTAVIEVNPEPTPLSGSATISIRESASQALPGLLERLPALLK
|
NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form.
|
P66814
|
Q9RSL5
|
RS14_DEIRA
|
30S ribosomal protein S14
|
Deinococcus
|
MANKSKLAKQKQREKTVEKYAAKRAELKAAGDYYGLTQLPRDASPTRLHNRCEFTGRPRGYVRFFGVSRIVLREMAHRGELPGVKKASW
|
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.
|
Q9RSL5
|
A4WW84
|
SECA_CERS5
|
Protein translocase subunit SecA
|
Cereibacter
|
MLGLGTLARKIFGTPNDRKVKSVRSLVARINELETEFQALSDEGIKQKTAEFQRRVQEGGESLDDLLPEAFANCREGARRALGLRAFDVQLMGGIFLHQGNIAEMKTGEGKTLVATFPAYLNALAGKGVHVVTVNDYLAKRDSEWMGKVYAQLGLTTGVVYPFQSEEEKKAAYRADITYATNNELGFDYLRDNMKASKEEMKQRGHFFAIVDEVDSILIDEARTPLIISGPSQDRSDLYTKVDKLIPELVEEHYKLDEKTRNVTFTEEGNEFLETRLHETGLLPEGQSLYDPESTTIVHHVNQGLRAHKLFHRDQQYIVRNDEIMLIDEFTGRMMRGRRLSDGLHQAIEAKEGVSIQPENVTLASVTFQNYFRLYDKLGGMTGTAATEAEEFMEIYGLGVVEVPTNRPVARTDEHDAVYRTAREKNDGIVASIKEAHERGQPILVGTTSIDKSEALSELLKAAGIPHNVLNARQHEQEAQIVADAGKPGAVTIATNMAGRGTDIQLGGNVEMKVMQALAADPTAHPDEIRARIEAEHAEEKQKVIDAGGLFVLGTERHESRRIDNQLRGRSGRQGDPGRSAFFLSLEDDLMRIFGSDRLDKVLSTLGMKDGEAIVHPWVNKSLEKAQAKVEARNFDIRKQLLKFDDVMNDQRKAIFSQRLEIMEAEDLSDIAQDMRYQVIDDLIDMHMPPKSYSDQWDIEGMHRAVMDKLGLDAPLAKWAQEEGVDQDVVRERLCEAADRQIADKTAAFGPETMRSIEKQILLQAIDAKWREHLLTLEHLRSVVGFRGYAQRDPLSEYKTEAFALFESMLNSLRQDVTQKLAQVRPLSEEEQQAVMRQFLDQQRTAAEAPASVPQPQAAVAPQPAPELVGADNGESQPQAWGDVARNDPCPCGSGLKYKHCHGRLD
|
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.
|
A4WW84
|
B9DM53
|
RS13_STACT
|
30S ribosomal protein S13
|
Staphylococcus
|
MARIAGIDIPREKRVVISLTYIYGVGKSTAAKILEEANVSPDTRVKDLTDDELGRIRETVDAYKVEGDLRREQNLNIKRLMEISSYRGIRHRRGLPVRGQKTKNNARTRKGPVKTVANKKK
|
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites.
|
B9DM53
|
O31618
|
THIG_BACSU
|
Thiazole synthase
|
Bacillus
|
MSMLTIGGKSFQSRLLLGTGKYPSFDIQKEAVAVSESDILTFAVRRMNIFEASQPNFLEQLDLSKYTLLPNTAGASTAEEAVRIARLAKASGLCDMIKVEVIGCSRSLLPDPVETLKASEQLLEEGFIVLPYTSDDVVLARKLEELGVHAIMPGASPIGSGQGILNPLNLSFIIEQAKVPVIVDAGIGSPKDAAYAMELGADGVLLNTAVSGADDPVKMARAMKLAVEAGRLSYEAGRIPLKQYGTASSPGEGLPV
|
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.
|
O31618
|
A4WSH8
|
CLPP_CERS5
|
Endopeptidase Clp
|
Cereibacter
|
MKDPIDLYMNTLVPMVVEQTSRGERAYDIFSRMLKERIIFLSGPVHDGMSSLICAQLLFLEAENPSKEIAMYINSPGGVVTSGLSIYDTMQYIRPKVSTLVIGQAASMGSLLLTAGEKGMRFSLPNSRVMVHQPSGGYQGQATDIMIHARETEKLKRRLNEIYVKHTGQDLDTVEAALERDNFMSAEDAKAWGLIDEILESRGKTDDTAK
|
Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
|
A4WSH8
|
A3M3H0
|
ATA_ACIBT
|
Type 5 secretion system autotransporter Ata
|
Acinetobacter calcoaceticus/baumannii complex
|
MNKVYKVIWNASIGAWVATSEIAKSKTKTKSKTLNLSAAVLSGVICFAPNAFAGTNTEGGIGQGTSISGTTSCREGSANTANQKDIAIGCGAQTQDRTGSNIANRNNPYNNSTGAYAGAMKQGGAISVGTGAVVEKGLGTAIGSYATTQGISGVAIGTGALSSGNTALAVGRQSAATADFSQAIGNVAAATGKGSLAIGHSATAEGYRSIAIGSPDIENADPVAGQAGAAYQPKMATKATGKDSIAFGGGAVATEENALAIGAFSESKGKKSVAIGTGAKAQKDNAVVIGDQAEASFEGGVAIGKGARSEAENSIALGKDSKASQATGESFLTKQSAPTGVLSIGDIGTERRIQNVADGAADSDAATVRQLKAARTHYVSINDNGQPGGNFENDGATGRNAIAVGVNASAAGREAMAIGGNAQAIGSGAIAMGSSSQTVGRGDVAIGRNASTQGAEGVNSNQSVAIGDQTKAIGDQSVAIGADVIAKGNSSVAIGGDDVDKIARDTELSNTYTEITGGTLQAGKYPTTEANHGSTAVGVQAVGTGAFSSAFGMTSKATGDASSAFGVMSNASGKGAAAFGAVAQATGDGASAMGINSLASGTNSTAIGSGNKPGEGANATGNSSAAIGSGAQATGDNSAAIGKGAEATNENAAAVGGGAKATGKNAAAIGGGAIADQENAVAVGQGAQSLVEGGVALGARSKVEAKNSVALGQDAVATEATGTSFLTNRDASQSNGVISVGSAGKERRITNVEDGSADSDAVTVRQLKNVDSRVNQNTSNIGKNTQNITNLNQKLDDTKTNLGNQIADTNKNLNDAKKDLGNQITDTNTKLNTTKDQLTTQINDTNTELNNTIGNTKTELNTKIDNTKTELENKGLNFAGNSGADVHRKLGDKLNIVGGAAASTPAAKTSGENVITRTTQDGIQIELLKDSKFDSVTTGNTTLNTNGLTIKEGPSITKQGINAGSKQISNVADGINAKDAVNVDQLTKVKDNLNGRITDTNNQLNDAKKDLGNQIADTNKNLNDAKKDLGNQITDTNTKLNNTKDQLTTQINDTKTELNNTIGNTKTELNSKIDSTKTELENKGLNFAGNSGADVHRKLGEKLNIIGGAAASTPAAKTSGENVITRTTKDGIQIELLKDSKFDSVTTGNTTLNTNGLTIKEGPSITKDGINASGKQITNVADGVNAKDAVNKGQLDNLAAKQNATDDAAVKYDDAKTKDKVTLKGKDGTVLDNVKAGHISSTSKEAVNGSQIHNISNSIKNSIGGNTVVNPDGSLTTNNIGGTGKNNINDAISEVKNTATKAKTTVTEGDNIVVKETVNKDGSTNYEVSTKKDLTLNSVTTGDTVLNNNGLTIKDGPSITKDGVNAGGKKITDVANGVIAQNSKDAVNGAQVHHISNSIKNSIGGNTVVNPDGSLTTNNIGGTGKNNINDAIKSVDEKVTNGVNDLTQKGLNFGANDQKTTQGKAVHRKLGDTINIVGGADAKTAEDKTSGENIITRTTEDGVKIEMLKDVKFDSVNVGGHVLNQQGLIIKGGPSITVNGINAGGKQITNVADGINAKDAVNKGQLDKQINEVKDQIGKDIGKLSDHAVQYDKDKNGNVDKSSVTLGGGEKGTNLKNVADGKVAEGSKDAVNGGQLWNVQNQVDKNSNDIKNIQNNIDNISNGKAGLVQQQKPNGEITVGRDTGGTSINMAGKEGDRVVQGVKDGEIKAGSNQAVNGGQIHKISESIKNSIGGNTTIDPKDGSITTNNIGGTGKNNINDAIGTLNQSNQELGNKITNLGDQLQQVFYDTNKRIDDVEKKANAGIAAAMALENAPFVAGKYTYAVGAAYHGGENAVGVTLRKTSDNGRWSITGGVAAASQGEPSVRVGISGVIN
|
Important for biofilm formation, binding to various extracellular matrix/basal membrane (ECM/BM) proteins, adhesion to collagen type IV, and for survival in a mouse model of lethal infection.
|
A3M3H0
|
Q9RFN0
|
BGAL_CARML
|
Beta-galactosidase BgaB
|
Carnobacterium
|
MLQQKKLFYGGDYNPEQWSKAIILEDMRLMKKANVNYVSLNIFGWASIQPTEEGFDFSFLDEMLDLLWENGIGIDLANGTASPPAWLVKKHPEILPVTSQGTPLVHGSRQHYCPSNKVYRSYVIRLTEEVAKRYATHPGIVMWHVNNEYTCHISECYCESCEKSFRQWLQMKYKKINTLNECWSTKFWSQSYSQWDEIFLPKEMPTFKNPAHQLDYKRFISDQNLTLFKAEKKAIRSYSKDIPVMTNLMGLHKHVDGFAFAEEMDVVGWDSYPNPFEEKPYPQFLANDLTRSLKKKPFLVMEQAPSAVNWRRANGAKSPGQMRLWSYEALAHGADGILFFQWRQSQGGAEKFHSGMVSHNQDTNSRIFKEVVQLGTEMSQLDELVGTNYNAEVAIVFDWENWWALELDAKPSGEINYIKQMRDLYTIFHELNIGVDFIHPKEDLSNYKLVLSIAQYLVTDDFSAKVKRYIKAGGHFLTTFFSGIVDEYDRVYLGGYPGAFKEVLGIYVEEFDPMPIGRKSQIKYGETYYTTELWKEVIHLQGAETIATFTEGYLMGQPALTKFGYGKGKTYYMGTKLAKDGNMKFIQTILAESKIQPLNQVEIESENSKISMTCRSNSSHDYIFLLNYGQTSEKVKLKKGGQSLLDGSMVEGEVSVKANDVKIIKLTK
|
Capable of hydrolyzing the chromogen 5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-Gal) at low temperatures. pNP-beta-galactoside, pNP-beta-fucoside and pNP-beta-galacturonide are also hydrolyzed, but not pNP-beta-galactosidase, pNP-alpha-galactoside, pNP-beta-mannoside, pNP-beta-arabanoside, pNP-beta-xyloside, pNP-beta-glucuronide nor pNP-betacellobioside at 20 degrees Celsius.
|
Q9RFN0
|
B0SH16
|
RIMP_LEPBA
|
Ribosome maturation factor RimP
|
Leptospira
|
MVYTEENIRELILRVLAPPLALFSLQVQNRKNHALIEIELDHLTDKTGSASLEDCETVSRRLKEELDQWGEEFDFTLQVSSAGAERVLRLPEDLIRFQGLLVKLEVPLESGKWDKRLYRLGPVSGDSVELTLYDRKTRHKKNQKSVSMPIAEIRKGNLYLEI
|
Required for maturation of 30S ribosomal subunits.
|
B0SH16
|
A1S4B5
|
GLYA_SHEAM
|
Serine hydroxymethyltransferase
|
Shewanella
|
MLKKTMNIADYDPELFKAIEDETLRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDIVETLAIERAKELFGATFANVQPHSGSQANSAVYMTLLQPGDTVLGMNLAHGGHLTHGSPVNFSGKLYNIIPYGIDETGKIDYDEMERLAVEHKPKMMIGGFSAYSGIVDWARMREIADKIGAYLFVDMAHVAGLVAAGVYPNPVPHAHVVTSTTHKTLAGPRGGIILSAANDEDLYKKLNSAVFPGGQGGPLMHVIAGKAVAFKEALEPEFKVYQQQVVTNAKAMVEVFLERGYKIVSGGTDNHLMLVDLIGRDLTGKEADAALGAANITVNKNSVPNDPRSPFITSGIRIGTPAITRRGFKEAEARELTHWICDVLDNAKDESVIARVKGQVLELCARFPVYG
|
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.
|
A1S4B5
|
P24309
|
DBR1_YEAST
|
Lariat debranching enzyme
|
Saccharomyces
|
MTKLRIAVQGCCHGQLNQIYKEVSRIHAKTPIDLLIILGDFQSIRDGQDFKSIAIPPKYQRLGDFISYYNNEIEAPVPTIFIGGNHESMRHLMLLPHGGYVAKNIFYMGYSNVIWFKGIRIGSLSGIWKEWDFNKQRPDWNDLENNNWKANIRNLYHVRISDIAPLFMIKHRIDIMLSHDWPNGVVYHGDTKHLLKLKPFFEQDIKEGKLGSPVTWQLLRDLRPQWWLSAHLHVRFMASIKHNKRSHEPPNKSTSKTKKNNNEIDLDLSSDEDERSGIMNCQEENEYDSKYGETRFLALDKCLPRRRWLEILEIEPDTSHASWKDENHRMFWDPEFINNLVICQKNKNLLSNKPFNSVNWIELSQSNREEGRDIDWENYAIPAYTLDIQKDEVRQTKAFISKFMT
|
Cleaves the 2'-5' phosphodiester linkage at the branch point of lariat intron pre-mRNAs after splicing and converts them into linear molecules that are subsequently degraded. It thereby facilitates ribonucleotide turnover. It also participates in Ty1 retrovirus-like transposition via an RNA lariat intermediate in cDNA synthesis.
|
P24309
|
Q9D7H2
|
WDR5B_MOUSE
|
WD repeat-containing protein 5B
|
Mus
|
MATEHLPAERAQSLLSAPRREEEPQKPNYALRLTLAGHSAAISSVKFSPNGEWLASSAADALIIIWGAYDGNCKKTLYGHSLEISDVAWSSDSSRLVSASDDKTLKVWDMRSGKCLKTLKGHSDFVFCCDFNPPSNLIVSGSFDESVKIWEVKTGKCLKTLSAHSDPISAVNFNCNGSLIVSGSYDGLCRIWDAASGQCLRTLADEGNPPVSFVKFSPNGKYILTATLDNTLKLWDYSRGRCLKTYTGHKNEKYCLFASFSVTGRKWVVSGSEDNMVYIWNLQTKEIVQRLQGHTDVVISAACHPTKNIIASAALENDKTIKVWSSDC
|
May function as a substrate receptor for CUL4-DDB1 ubiquitin E3 ligase complex.
|
Q9D7H2
|
Q030K6
|
RIMP_LACLS
|
Ribosome maturation factor RimP
|
Lactococcus cremoris subsp. cremoris
|
MNDVVKIVEDFIKPHIPKPFELFAVEWEKFGGDMMLSILVDKEGGIEIDETAELSELISPLLDTISPDPFPTEGYLLEVASPGAERPLRKAEHFAGAVGEYIFVKLYQKINNEKEFTGDLVSFDGENLVVDVLDKTRHKNIEIPLSAVAKAQTMVKF
|
Required for maturation of 30S ribosomal subunits.
|
Q030K6
|
P06250
|
PETD_MARPO
|
17 kDa polypeptide
|
Marchantia
|
MGVTKKPDLSDPILRAKLAKGMGHNYYGEPAWPNDLLYIFPVVILGTIACTVGLAVLEPSMIGEPANPFATPLEILPEWYFFPVFQILRTVPNKLLGVLLMAAVPAGLLTVPFLENVNKFQNPFRRPVATTVFLIGTVVALWLGIGAALPIDKSLTLGLF
|
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.
|
P06250
|
P42156
|
CASK_CAPCR
|
Kappa-casein
|
Capricornis
|
MMKSFFLVVTILALTLPFLGAQEQNQEQPICCEKDETFFDDKIAKYIPIQYVLSRYPSYGLNYYQQRPVALINNQFLPYPYYAKPVAVRSPAQTLQWQVLPNTVPAKSCQDQPTTMARHPHPHLSFMAIPPKKDQDKTEIPTINTIASAEPTVHSTPTTEAIVNTVDNPEASSESIVSAPETNTAQVTSTEV
|
Kappa-casein stabilizes micelle formation, preventing casein precipitation in milk.
|
P42156
|
Q8Q009
|
CHEB1_METMA
|
Protein-glutamate methylesterase/protein-glutamine glutaminase 1
|
Methanosarcina
|
MNEFGDSMIRTLIVDDSAFMRMAIRSMLASSPDIKIAGDACNGKEAVDKSKSLHPDIIIMDVNMPVMDGLTAVKTIMSTDPVPIIMFSTLTVEGSKEALEALQLGAIDFVPKSESHHDVNKIEKELVDKIRNIHSSNPSILRLINMRKFKGEVVRGKWSCAGDFAVLIGSSTGGPSSLEQVIPRLPGDLPAPVFVVQHMPEGNFCKQLAERLNFLSELEIKEARNNEKVTAGVVYIAPGGYHMTVKKALGVTRIKLIKSQPVHAVMPAVDVIAESMLDVYGKNIVAAILTGMGFDGAAGFKKIRDAGGSTIACSEDTCVIFGMPKAAIAAGGIDTVKPIFEIPEEIVRMSEVKCNGK
|
Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.
|
Q8Q009
|
P30343
|
MER3_STRLI
|
Mercury resistance operon ORF3
|
Streptomyces
|
MTSPSPTARRTRLRRRTALALAAAATAALTLSACGTDTKANTPATRAGSGNAAAAKADTVALLDDTTLAVPGDKPSALFFFSVGCGECAGGAKSLDKAAQAFDKAGKKANFLAVDMDPNESKQTIMQFLDYIKAPALPATIDKGAALSQRYQVAALSTLIVVAPQGKVTYRATDPSADQIQDALKKAGA
|
Probable mercury binding protein.
|
P30343
|
Q3ITC8
|
VATA_NATPD
|
V-ATPase subunit A
|
Natronomonas
|
MSQATASEITDEGVIESVSGPVVTAVDLDARMNDVVYVGEEGLMGEVIEIEGNLTTIQVYEETSDVAPGEPVENTGEPLSVDLGPGMMDSIYDGVQRPLDVLEEKMGAFLDRGVDAPGIDLEKTWEFNPEVSEGDEVSPGDVVGIVPETESIDHKVLVPPDYEGGEVTAVESGNFTVDETVVELDSGEEIQMRQEWPVREPRPTVEKETPTTPLVSGQRVLDGLFPIAKGGTAAIPGPFGSGKTVTQHQLAKWADADIVVYVGCGERGNEMTEVIEDFPELEDPKTGKPLMSRTCLIANTSNMPVAARESCVYTGITIAEYYRDMGYDVALMADSTSRWAEAMREISSRLEEMPGEEGYPAYLAARLSEFYERAGKFQNMNGSEGSISVIGAVSPPGGDFSEPVTQNTLRIVKCFWALDADLAERRHFPSINWNESYSLYKEQLDPWWRENVHEEFPEVRQWAVDVLDEEDELQEIVQLVGKDALPEDQQLTLEVARYIREAWLQQNAFHDVDTYCEPEKTYQMLTAIQHFNDEAFEALDAGVPVEEIIDVDAVPQLNRMNTQEDYEEYIEELKGDLTDQLRELY
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal alpha chain is a catalytic subunit.
|
Q3ITC8
|
O64644
|
SAP18_ARATH
|
18 kDa Sin3-associated polypeptide
|
Arabidopsis
|
MAEAARRQGGGRPLPPPPRGVNQQPPRPKPEPVDREKTCPLLLRVFTKSGGHHTSEDYAVRGKEPKDEVQIYTWKDASLRELTDLVKEVSVAARRRNARLSFAFVYPNNKGGYNVREVGETMAYPNRKQPDDSKTLSELPFEIGDYLDVAIY
|
Links the histone deacetylase complex to transcriptional repressors bound to chromatin. Involved in the tethering of the SIN3 complex to core histone proteins.
|
O64644
|
Q54R41
|
GPA9_DICDI
|
Guanine nucleotide-binding protein alpha-9 subunit
|
Dictyostelium
|
MGCNSSSEAKQSDKIDRTLYDEKKSQEREIKLLLLGSGDSGKSTIAKQMRYIHTKGFSNEEIATFVEIMHSNVLSSIQILIRNVPVEQLGSDLKDKANYYSSINPYELPLTPDIGLEIDRLWKNEAIQKLFSTNRAELNLPEVTAYCLDQVERISSETYTPTQEDVLRCRQRTTGMKETQFNVEDIKFRLIDVGGQKNERRKWMHYFEDVKSIIFCVALGDYDMNLVEDETINRMEDSLKLWNDIVNNPFFKNTSFVLFLNKNDIFREKIKKIPLVDYFPDYQGGYNYEKGIEYIRNKFFSSVPTATTIVAHVTTATDTENITIVFDAVRRNIIQSILKLHY
|
Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. G alpha-9 antagonizes broad chemotactic response. It functions rapidly following receptor stimulation to negatively regulate PI3K/PTEN, adenylyl cyclase, and guanylyl cyclase pathways.
|
Q54R41
|
A0Q323
|
DDL_CLONN
|
D-alanylalanine synthetase
|
Clostridium
|
MKKKVAILFGGQSTEHEVSRVSASSVLKNIDLSKYDVYPIGITKDGKWFEYTGAIDKIESGEWEKDEFYKNPNGQEILFNREVDVVFPVMHGLYGEDGTIQGLCKLLTIPCVGPGVMSSAVCMDKVYTKYVLENFGVKQADYVVVNAHDYKNNKMDIISTIENKLGYDVFIKPSNSGSSVGISKAHNREELEAGLEEALKFDRKVLVEVALNAREIEVAVLGNDEPVAATPGEIVPANEFYDYEAKYSNAQSKLLLPANLSPEKLEKVKELAVRIFKMLDCAGMSRVDFLVDKETEEVYLNEINTIPGFTKISMYPKMWQAEGKAYGELISEIIELAVERDNK
|
Cell wall formation.
|
A0Q323
|
A1RH89
|
DEOB_SHESW
|
Phosphodeoxyribomutase
|
Shewanella
|
MKRTIIMMLDSFGVGASADAASFGDVGSDTFGHIAKACAEGKADIGREGPLKLPNLARLGLGHAAMESTGAFAPGFGDNVELIGAYGHAQELSSGKDTPSGHWEMAGVPVLFEWGYFSEHQNSFPKELTDKILARAGLDGFLGNCHASGTTILEELGEEHMRSGKPIFYTSADSVFQIACHEETFGLDNLYRLCEITREELAPYNIGRVIARPFNGTGPSDFARTGNRKDYSLEPPAKTVLDKLKAAGGEVVSVGKIADIYAYCGITKKVKANGLEDLFDATLAEVKSAGDNTIVFTNFVDFDSHYGHRRDVAGYAKGLEYFDARLPEMLALLGEDDLLILTADHGCDPTWQGTDHTREYVPVLAYGAGLKAGSLGRRNSFADIGQSIASHFKLEPMAYGESFI
|
Phosphotransfer between the C1 and C5 carbon atoms of pentose.
|
A1RH89
|
Q31L13
|
RS3_SYNE7
|
30S ribosomal protein S3
|
Synechococcus
|
MGQKINPVGFRLGVTQEHRSRWFADPNRYPQLLQEDKKIRDYVRKNLSNAGIADIRVERKADQVELEIRTARPGVVVGRGGAGIDTLREGLQALLKDSSRQIRINVIEVERVDADAALLGEYIAQQLERRVAFRRCVRQAIQRAQRAGVQGIKIQVAGRLNGAEIARTEWTREGRVPLHTLRADIDYAYTTATTTYGILGIKVWVFRGEIIPGQEDAAPSNVGQPRRRNQQRRRQQFEDRSNEG
|
Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.
|
Q31L13
|
A5CXX4
|
RIMP_VESOH
|
Ribosome maturation factor RimP
|
Candidatus Vesicomyosocius
|
MARVTDKITHLIKPVIEGMGYELLGIEYVASGKYSILRIFIDTNKSISVNDCEIVSRQLSSIFDIEEPISGQYNLEVSSPGIERPLFHKGHYQCFLGFNVKLHMFRPISGQSNFFGVIGSVSEINNTIELVGELGAIILDIDLIKKANLVVDF
|
Required for maturation of 30S ribosomal subunits.
|
A5CXX4
|
Q9BDI9
|
LSHB_PANTA
|
Luteinizing hormone subunit beta
|
Panthera
|
MEMLQGLLLLWLLLNVGGVWTSRGPLRPLCRPINATLAAENEACPVCVTFTTTICAGYCPSMMRVLPAALPPVPQPVCTYRELRFASVRLPGCPPGVDPVVSFPVALSCRCGPCRLSSSDCGGPRAQPLACDRPPLPGLPFL
|
Promotes spermatogenesis and ovulation by stimulating the testes and ovaries to synthesize steroids.
|
Q9BDI9
|
Q33645
|
CYB_ANGAN
|
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
|
Anguilla
|
MANLRKTHPLLKIANDALVDLPTPSNISAWWNFGSLLGLCLISQILTGLFLAMHYTSDISTAFSSVAHICRDVNYGWLIRNLHANGASFFFICLYLHIARGLYYGSYLYMETWNIGVVLFLLVMMTAFVGYVLPWGQMSFWGATVITNLLSAVPYVGNSLVQWIWGGFSVDNATLTRFFAFHFLFPFVVAGATMLHLLFLHETGSNNPVGLNSDADKIPFHPYFSYKDLLGFIIMLTALTMLALFYPNLLGDPDNFTPANPMVTPPHIKPEWYFLFAYAILRSIPNKLGGVLALLSSILVLMVVPILHTSKQRGLTFRPASQLLFWILVADMLVLTWIGGMPVEHPYIIIGQVASVLYFSLFLVLNPLVGWLENKVMNW
|
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
|
Q33645
|
Q8L7E3
|
VSR7_ARATH
|
Epidermal growth factor receptor-like protein 3
|
Arabidopsis
|
MGLVNGRASLTFLLAALTIIAMVVEARFVVEKESISVLNPEEMRSKHDGSIANFGLPDYGGFLIGSVVYPDSKTDGCSAFGKTFKPKFPRPTILLLDRGGCYFALKAWHAQQAGAAAVLVADNVDEPLLTMDSPEESKDADGFIEKLTIPSVLIDKSFGDDLRQGFQKGKNIVIKLDWRESVPHPDKRVEYELWTNSNDECGARCDEQMDFVKNFKGHAQILEKGGYTAFTPHYITWFCPFQFINSPHCKSQCINHGRYCAPDPEDNFREGYEGKDVVLENLRQLCVHRVANESSRPWVWWDYVTDFHSRCSMKEKKYSIDCAESVIKSLNLPIEKIKKCIGDPEADTENQVLRTEQVSQIGRGNRGDVTILPTLVINNAQYRGRLERTAVLKAICAGFNETSEPAICLNTGLETNECLENNGGCWQDTKANITACQDTFRGRLCECPVVKGVQYKGDGYTSCTPYGPARCTMNNGGCWSDTRNGLTFSACSDSVSTGCKCPEGFQGDGLTCEDINECKERSVCQCSGCRCKNSWGGYKCSCSGDRLYINDQDTCIERYGSKTAWWLTFLILAIVAVAGLAGYIFYKYRFRSYMDSEIMTIMSQYMPLESQRAREVPSEAEPFTL
|
Vacuolar-sorting receptor (VSR) involved in clathrin-coated vesicles sorting from Golgi apparatus to vacuoles.
|
Q8L7E3
|
Q8YPJ6
|
RL15_NOSS1
|
50S ribosomal protein L15
|
Nostoc
|
MRLNDVKPQKGSKKRRRRVGRGISAGQGASAGLGMRGQKSRSGSGTRPGFEGGQQPLYRRIPKLKGFPVVNRKIYTTINVEKLADLPANTEVTLESLRAAGILTAAKGPLKILGNGDLGVALNVKAAAFTGQARSKIEAAGGSCEVLG
|
Binds to the 23S rRNA.
|
Q8YPJ6
|
Q7VNT3
|
RNFD_HAEDU
|
Rnf electron transport complex subunit D
|
Haemophilus
|
MFKMVSSPHTHGTNLTAKFMLWVIVAMLPALIVQIAFFGTGVVIQLAIALSMAIVIEIVVAKLRHKSTTFYLADLAGVVTATILAMAIPPYAPYWVVMIGMIVALLLAKHCYGGLGQNLFNPAMVAYAFLLISFPVQMTSWLPSFELLAEPPTFKDAWLLIFKGVTSDGFTSRQLLSGIDGIAQATPLDSAKTSIAKLGFDGVIQSPIFSGIFARGWLQLNLAFLAGGLFLLYKRIIHWQIPVAMLVVFSVLSALTDLVTMHTHLNVLSQLFSGAMMFGAFFIATDPVSASITPKGKLIFGGLIGLLAYLIRYYGSYPDAIAFAVLLANLCVPLIDHYTQPRLYGTHK
|
Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
|
Q7VNT3
|
A4FZP0
|
IF2B_METM5
|
eIF-2-beta
|
Methanococcus
|
MVDYFDYNSLLTRAREQLPEEVFKDVRFEIPSADSFVEGNRTIIKNFKDIAKFMERDAQEFAKYVMKELGTAGDIEGVRLILQGKFGWRMVNEKIQNYVNEYVLCPECGKPDTKIVKEGRIHFLKCTACGAMKPVKTL
|
eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.
|
A4FZP0
|
Q90352
|
AVT_CATCO
|
[Arg8]-vasotocin receptor
|
Catostomus
|
MGRIANQTTASNDTDPFGRNEEVAKMEITVLSVTFFVAVIGNLSVLLAMHNTKKKSSRMHLFIKHLSLADMVVAFFQVLPQLCWEITFRFYGPDFLCRIVKHLQVLGMFASTYMMVMMTLDRYIAICHPLKTLQQPTQRAYIMIGSTWLCSLLLSTPQYFIFSLSEIQNGSYVYDCWGHFIEPWGIRAYITWITVGIFLIPVIILMICYGFICHSIWKNIKCKTMRGTRNTKDGMIGKVSVSSVTIISRAKLRTVKMTLVIVLAYIVCWAPFFIVQMWSVWDENFSWDDSENAAVTLSALLASLNSCCNPWIYMLFSGHLLYDFLRCFPCCKKPRNMLQKEDSDSSIRRNTLLTKLAAGRMTNDGFGSWRDPCNSRKSSQSIGLDCFCKSSQCLEHDCSRKSSQCIPLDCSRKSSQCIPLDCSRKSSQCMSKES
|
Binds to vasotocin. Produces an induction of membrane chloride currents indicating that it is coupled to the inositol phosphate/calcium pathway.
|
Q90352
|
Q8WZ55
|
BSND_HUMAN
|
Barttin
|
Homo
|
MADEKTFRIGFIVLGLFLLALGTFLMSHDRPQVYGTFYAMGSVMVIGGIIWSMCQCYPKITFVPADSDFQGILSPKAMGLLENGLAAEMKSPSPQPPYVRLWEEAAYDQSLPDFSHIQMKVMSYSEDHRSLLAPEMGQPKLGTSDGGEGGPGDVQAWMEAAVVIHKGSDESEGERRLTQSWPGPLACPQGPAPLASFQDDLDMDSSEGSSPNASPHDREEACSPQQEPQGCRCPLDRFQDFALIDAPTLEDEPQEGQQWEIALPNNWQRYPRTKVEEKEASDTGGEEPEKEEEDLYYGLPDGAGDLLPDKELGFEPDTQG
|
Functions as a beta-subunit for CLCNKA and CLCNKB chloride channels. In the kidney CLCNK/BSND heteromers mediate chloride reabsorption by facilitating its basolateral efflux. In the stria, CLCNK/BSND channels drive potassium secretion by recycling chloride for the basolateral SLC12A2 cotransporter.
|
Q8WZ55
|
Q7N7B2
|
PROB_PHOLL
|
Gamma-glutamyl kinase
|
Photorhabdus
|
MMNSSQTLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQQHEKGHRIIIVTSGAIAAGREHLGYPDLPATIASKQLLAAVGQSRLIQLWEQFFSIYGIHVGQMLLTRADLEDRERFLNARDTLQALLDNRIVPVINENDAVATAEIKVGDNDNLSALAAILGGADKLLLLTDIEGLYTADPRNNPDAKLIPEVYDISDELRMVAGDSISGLGTGGMATKLQAAGIAGRAGIDVIIAAGNKPDVISDVIEGNPVGTRFHGLESPMENRKRWIFGAPPAGEIIVDHGAETAICEKGSSLLPKGIKNIKGDFSRGEVICIRSLSGKDLAHGVCRYNSDALRLIAGHHSQQISQILGYEYGAVAVHRDDMIVS
|
Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
|
Q7N7B2
|
Q5QIT3
|
2AB2B_ARATH
|
Serine/threonine protein phosphatase 2A regulatory subunit B'' beta 1 isoform
|
Arabidopsis
|
MVDTVIPGDMACLDADLLQLQEMSSFVLNSKPGFTQKLFDQWLSLPEAQRQVGSLLKDAVAGAPINVTGSASGSNSATIPSMFPAGSAPPLSPRSCGSPRTTKQRAPSNLGSTLKVVNEPVKEPIPQFYFQNGRPPPSEIKEQCMFRINHFFYGHMDGLQIQEFKLVTREICKLPSFFSTSLFRKIDLNNTGFVTRDAFIDFWVNGNMLIMDTTTQIFKILKQKDQSFIVKDDFKPLLKELLATHPGLEFLQSTPEFQERYAETVTYRIFYYINRSGNGRITFRELKRGNLIDAMLHADEEEDINKVLRYFSYEHFYVIYCKFWELDTDHDFLIDKENLMRYGNHALTYRIVDRIFSQVARKFTSKVEGKMGYEDFVYFILAEEDKSSVPSLEYWFKCIDLDANGIITRNEMQFFYEEQLHRMECMAQEAVLFEDILCQMIDMIGPENESHITLHDLKGSKLSGNVFNILFNLNKFMAFETRDPFLIRQERENPTLTDWDRFAHREYIRLSMEEDVEDASNGSAEVWDDSSLEAPF
|
Regulatory subunit of type 2A protein phosphatase. Involved in post-transcriptional regulation of HMGR but not in root growth regulation in response to salt.
|
Q5QIT3
|
Q8WI17
|
YCF3_PSINU
|
Photosystem I assembly protein Ycf3
|
Psilotum
|
MPRSQRNDNFIDKTFTIAADILLRVIPTTRREKEAFTYYRDGMSAQSEGEYAEALQNYYKAMRLEIDPYDRSYILYNIGLIHTSNGEHAKALEYYFQALERNPSLPQAFNNMAVICHYRGEQAIQQGDPGTSEIWFDKAAEYWKQAIALAPNNYIEAQNWLRITGRSEDWE
|
Essential for the assembly of the photosystem I (PSI) complex. May act as a chaperone-like factor to guide the assembly of the PSI subunits.
|
Q8WI17
|
Q5GJ04
|
FSHR_FELCA
|
Follitropin receptor
|
Felis
|
MTFLLVSLLAFLSLGSGCHHRICHCWHRVFLCQESKVTEIPSDLPRNAVELRFVLTKLRVIPKGAFSGFGDLEKIEISQNDVLEVIEANVFFNLSKLHEIRIEKANNLLYIDTDAFQNLPNLRYLLISNTGIKHFPAVHKIQSLQKVLLDIQDNINIHTVERNSFMGLSFESMILWLNKNGIQEIHNCAFNGTQLDELNLSDNINLEELPNDVFQGASGPVILDISRTRIHSLPSYGLENIKKLRAKSTYNLKKLPSLDKFVALMEASLTYPSHCCAFANWRRPISELHPICNKSILRQEVDDMTQARGQRVSLAEDEESSYTKGFDMMYSEFDYDLCNEVVDVTCSPKPDAFNPCEDIMGYDILRVLIWFISILAITGNIIVLMILITSQYKLTVPRFLMCNLAFADLCIGIYLLLIASVDIYTKSQYHNYAIDWQTGAGCDAAGFFTVFASELSVYTLTVITLERWHTITHAMQLECKVQLRHAAIIMLLGWIFAFMVALFPIFGISSYMKVSICLPMDIDSPLSQLYVMSLLVLNVLAFVVICCCYAHIYLTVRNPNIVSSSSDTKIAKRMAMLIFTDFLCMAPISFFAISASLKVPLITVSKSKILLVLFYPINSCANPFLYAIFTKNFRRDFFILLSKFGCYEVQAQTYRSETSSTAHNFHPRNGHCPPAPRVTNSSNYILIPLRHLAKN
|
G protein-coupled receptor for follitropin, the follicle-stimulating hormone. Through cAMP production activates the downstream PI3K-AKT and ERK1/ERK2 signaling pathways.
|
Q5GJ04
|
P57839
|
YCIB_PASMU
|
Inner membrane-spanning protein YciB
|
Pasteurella
|
MKQLLEFIPLILFFAVYKLVGIREAAITLIIATLIQLLILKIKYGKVEKQQLFMGIAVVFFGTLTAYFNQLEYLKWKVTIVYAIFALVLLVSQYGFNKNLIKLMLGKEDALELPEQVWNRLNLGWALFFLLCMLINLYISQYLSDDLWVDFKTFGILGMTLIATIITGIYIYRYLPQTKSNNKE
|
Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis.
|
P57839
|
A7E3Q8
|
PLST_BOVIN
|
T-plastin
|
Bos
|
MDEMATTQISKDELDELKEAFAKVDLNSNGFICDYELHELFKEANMPLPGYKVREIIQKLMLDGDRNKDGKISFDEFVYIFQEVKSSDIAKTFRKAINRKEGICALGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELSRNEALAALLRDGETLEELMKLSPEELLLRWANFHLENSGWQKINNFSADIKDSKAYFHLLNQIAPKGQKEGEPRIDINMSGFNETDDLKRAESMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFNKYPALTKPENQDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLYADLQDALVILQLYERIKVPVDWSKVNKPPYPKLGANMKKLENCNYAVELGKHPAKFSLVGIGGQDLNDGNQTLTLALVWQLMRRYTLNVLEDLGDGQKANDDIIVSWVNRTLNEAGKSTSIQSFKDKTISSSLAVVDLIDAIQPGCINYDLVKSGTLTEDDKHNNAKYAVSMARRIGARVYALPEDLVEVKPKMVMTVFACLMGRGMKRV
|
Actin-bundling protein.
|
A7E3Q8
|
A8AEL8
|
PDUW_CITK8
|
Propionate kinase
|
Citrobacter
|
MSHKIMAINAGSSSLKFQLLAMPQGEMICQGLIERIGMANARVTMKTSAQKWQETAPIADHRESVTLLLDKLLSHHIINTLQDIDGVGHRVAHGGEFFKDSARVTDETLAQIERLAELAPLHNPVNALGIHIFRQLLPSTPSVAVFDTAFHQTLDESAYIYPLPWRYYTELGIRRYGFHGTSHKYVSTALAERLGVPLSALRVICCHLGNGSSICAIKGGQSVNTSMGFTPQSGVMMGTRSGDIDPSILPWIAEREGKTPQQLNYLLNNESGLLGISGVSHDYRDVEQAADGGNRRAALALTLFAERIRATIGSYIMQMGGLDALIFTGGIGENSARARAAVCHNLHFLGLSIDEEKNLRNATFIQAENAVVKVAVINTNEELMIAQDVMRIALSDKVTFGVSA
|
Works with phosphate acetyltransferase (pta) to capture exogenous propionate and regenerate propionyl-CoA during degradation of 1,2-propanediol (1,2-PD).
|
A8AEL8
|
A8GYY3
|
RL16_SHEPA
|
50S ribosomal protein L16
|
Shewanella
|
MLQPKRMKFRKMFKGRNRGLANGTEVSFGEFGLKAVGRGRLTARQIEAARRAMTRHIKRQGQIWIRVFPDKPITSKPLEVRMGKGKGNVEYWVCQIQPGKVLYEMNGVSEELAREAFTLAAAKLPLKTTFVTKSVM
|
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
|
A8GYY3
|
Q0IEN3
|
TRMB_AEDAE
|
tRNA(m7G46)-methyltransferase
|
Stegomyia
|
MEVEESKNDASVVASPAPTKLPQKRFYRQRAHSNPIADHSFDYPIHPDDYDWSQHYPTIGDKRVEFADIGCGYGGFLVTLGEMFPDKFAVGMEIRVKVSDYVMDRIQALRKLNEGQYENIACIRTNAMKYLTNFFHKGQLEKMFFLYPDPHFKKAKHKWRIINSALLSEYSYVLRQGGLIYTITDVKDLHEWMCKHIEQHPAFERLTDDEVKADVLSEKLLDSSEEGKKVTRNKGDKFVAIFRKI
|
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
|
Q0IEN3
|
Q8D935
|
RLMF_VIBVU
|
rRNA adenine N-6-methyltransferase
|
Vibrio
|
MTNKRKSAKPLEPAKRAPKPRTKKSRDLSASESNCDFVKVTRAGLHSRNKHQGRYDFAKLTQALPSLAPFVIKNPKGEASISFSDSTAVKMLNKALLSAYYQVANWDIPAGYLCPPIPGRADYIHRLAELLEGEVKGKFPHEKVQALDIGVGANAIYPIIAICDYRWRYTGSDVDPKSIESAQRIADSNPVLQGQLELKLQDQSQHIFQGIIGPTDYFHVTTCNPPFHASAQEAAFGTQRKLDNLAANRLKKGVTAKAGSQKISKNKPILNFGGQNSELWCQGGESSFLKRMANESERFAHQVLWFSTLVSKKDNVRPLRKQLEKLGVRSIRVVEMSQGQKVSRFVAWSFMDKQQRGEWIKLRG
|
Specifically methylates the adenine in position 1618 of 23S rRNA.
|
Q8D935
|
A9KNW4
|
IF2_LACP7
|
Translation initiation factor IF-2
|
Lachnospiraceae
|
MAKMKIHELAKELGVDNNVIVNFLQSKGSEVKSYRNNIEEKEIDLVRGKFKGSVSSNEPKSIDNGKASRVEKPEKNNSVTAKADQTPSEPVVHKQRPMTAQGERKNMSEQNVTTGSTESEDNIQSVGDRKYQHTDRRPQGNNGEGPQTSTNSGDRRPQGQGSYGDRRPQGQNSGDRRPYNGDRPQGQNSGDRRPYNGDRPQGQNSGDRRPYNGDRPQGQGNYGDRRPQGQNSGDRRPYNGDRPQGQGNYGDRRPQGQGSYGDRRPNSGDRPQGQGNYGDRRPQGQGSYGDRRPQGQGSYGDRPQGQGSYGDRPQGQGSYGDRRPQGQGSYGDRRPQGQGSYGDRPQGQGSYGDRRPQGQGSYGDRPQGQGNYGDRRPGGQGSYGDRRPQGQGSYGDRPQGQGNFGDRRPQGQGGYGGRPQGQGSYGGRPQGQGGYAGRSQGQGSFGGFNKDFDKDKDSGYTRSFDKKRTDPKSGEKSSIKSDLANELTKEQRAAAFNDKSRDRDRNRDRGRNNVEDGNIKSAKGKKDPNRKGAFIMPKPQQSLEKQDEIKTVIIPEVLTIKELADKMKVVPSVVVKKLFLAGKMVSINSEITFEEAEEIALGYEIIAEKEVLVNKVEELLKEDDEDENLMVKRPPVVCVMGHVDHGKTSLLDAIREANVTSREAGGITQHIGAYTVEVNGEKITFLDTPGHEAFTSMRMRGAKSTDIAILVVAADDGVMPQTVEAISHAKAAGVQIIVAINKIDKPSANIERVKQELTEHELIAEDWGGDTIFVPVSAHTKEGIDQLLEMIILTAEMGELKANPDRMARGIVIEAELDKGRGTVATILVQKGTLHVGDNIVIGSTYGKVRAMMDDKGRRVKEATPSTPVEILGLNAVPNAGEIFMATENEKEARNIADAFISQGKERLLADTKAKLSLDGLFSQIQAGNIKELNLIVKADVQGSVEAVKQSLVKLSNEEVAVRIIHGGVGAINESDVMLASTSNAIIIGFNVRPDNMAREIAEREKVDLRLYRVIYSAIEDVEAAMKGMLDPTFEEKVMGHAEVRQVFKASGLGTIAGSYVLDGKIVRGCSARITREGTQIFEGALASLKRFKDDVKEVNTGYECGLVFEKFNDIQEYDLVELYMMVEVPR
|
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
|
A9KNW4
|
Q9LYS9
|
B561H_ARATH
|
Protein b561A.tha8
|
Arabidopsis
|
MSLSSRATLVVLCCLFMLIPSFTTAATEQGLHARSRCESYSFNNGKSFRSCTDLLVLNSYLHFNYAQETGVLEIAYHHSNLESSSWISWAINPTSKGMVGAQALVAYRNSTSGVMRAYTSSINSYSPMLQESPLSLRVTQVSAEYSNGEMMIFATLVLPPNTTVVNHLWQDGPLKEGDRLGMHAMSGDNLKSMASLDLLSGQVTTTKSVNRNMLLVKQIHAIVNALSWGILMPIGVMAARYMKNYEVLDPTWFYIHVVCQTTGYFSGLIGGLGTAIYMARHTGMRTTLHTVIGLLLFALGFLQILSLKARPNKDHKYRKYWNWYHHTMGYIVIVLSIYNIYKGLSILQPGSIWKIAYTTIICCIAAFAVVMEILQFKKRWARLFFKKSKDVEADQPTVSVDVIGETEKAERKKASGGIEIQIENYNITKNFMIPSVFVISYPHTSPPLLAFHSYHHPSTSIAATAA
|
May act as a catecholamine-responsive trans-membrane electron transporter.
|
Q9LYS9
|
A6Q6Q7
|
MNMG_SULNB
|
Glucose-inhibited division protein A
|
unclassified Sulfurovum
|
MNYDVIVIGGGHAGIEASLASARMGVKTLLITILAEQIGASSCNPAIGGLAKGHLVREVDALGGEMGLCTDATGIQFRTLNASKGPAVRGSRAQIDMDEYRIYMRNVVLNTENLDVKQEIADGLIVEEGEVKGVTTQLGNRYTASKVIITAGTFLNGLIHIGDKKQTAGRQGEFASVELAEYLKGLGLNIGRLKTGTCARIDAKSVDTSVMEVQPGDTPPPPFSFRTDKSTFNPKQLPCYVAYTNERTHEIIESNFYRAPMFSGQIEGVGPRYCPSIEDKINRFRDRPRHQIFVEPQTIDETEYYINGMSTSLPIDVQLEMVRSVEGMKNAKIVRYGYAIEYDYVDPTELKHTLETKKIKGLYTAGQINGTTGYEEAAAQGLMAGINAALSIQGKEALILRRDEAYIGVLIDDLVTKGTKEPYRMFTSRAEYRLLLREDNADMRLSKYGKELGLLDDAYIAKFEEKQKNIEEALNYLQENYVTPTKEFLAKLEAIGAVKINDRTCWIDVIGRGDFNRDKLVSLLPEFDKYDDEVMGQILVEAKYSRYIEKQQMQIDQMKDMLKIKIPEDFTYKNVSGLSNEIVEKLEKANPTTLFAASEISGVTPAALEIIHVYIKMSQKGKI
|
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.
|
A6Q6Q7
|
Q5PAK7
|
NUOI_ANAMM
|
NDH-1 subunit I
|
Anaplasma
|
MRRVMVLFGVVIAGVKGFMLTLVSMFRPKVTLRYPSEKGPLSTRFRGEHALRRYDDGEERCIACKLCEAICPAQAITIEAAERGDGSRRTVRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEYATETREELMYNKEKLLCNGDVWEEALDFRIRKNRPYY
|
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.
|
Q5PAK7
|
Q14FJ4
|
VM2OC_ECHOC
|
Disintegrin ocellatusin
|
Echis
|
MIQVLLVTICLAVFPFQGSSKTLKSGNVNDYEVVNPQKITGLPVGAFKQPEKKYEDAVQYEFEVNGEPVVLHLEKNKGLFSEDYSETHYSPDGSEITTNPPVEDHCYYHGRVQNDADSTASISTCNGLKGFFTLRGETYLIEPLKVPDSESHAVYKYEDAKKKDEAPKMCGVTLTNWESDEPIKKASHLVATSEQQHFHPRYVQLVIVADHSMVTKNNNDLTALTTWIHQIVNDMIVMYRILNIHITLANVEIWSSGDLIAVTSSAPTTLRSFGEWRARNLVNRITHDNAQLITAVHLDNLIGYGYLGTMCDPQSSVAITEDHSTDHLWVAATMAHEMGHNLGMNHDGNQCNCGAAGCIMSAIISQYRSYQFSDCSMNEYRNYITTHNPPCILNQALRTDTVSTPVSENELLQNSVNPCYDPVTCQPKEKEDCESGPCCDNCKFLKEGTICKMARGDNMHDYCNGKTCDCPRNPYKGEHDPMEWPAPAKGSVLM
|
Inhibits ADP-induced platelet aggregation (IC(50)=168 nM). Inhibits alpha-5/beta-1 (ITGA5/ITGB1) integrin and induces the expression of a ligand-induced binding site epitope on beta-1 integrin subunit. Has a direct chemotactic stimulus on human neutrophils in vitro.
|
Q14FJ4
|
P0A459
|
T2D1_STRPN
|
Type-2 restriction enzyme DpnI
|
Streptococcus
|
MELHFNLELVETYKSNSQKARILTEDWVYRQSYCPNCGNNPLNHFENNRPVADFYCNHCSEEFELKSKKGNFSSTINDGAYATMMKRVQADNNPNFFFLTYTKNFEVNNFLVLPKQFVTPKSIIQRKPLAPTARRAGWIGCNIDLSQVPSKGRIFLVQDGQVRDPEKVTKEFKQGLFLRKSSLSSRGWTIEILNCIDKIEGSEFTLEDMYRFESDLKNIFVKNNHIKEKIRQQLQILRDKEIIEFKGRGKYRKL
|
An M and P subtype restriction enzyme that recognizes the double-stranded, methylated sequence 5'-G(Me)ATC-3' and cleaves after A-2.
|
P0A459
|
A0JMU5
|
ANM9_XENLA
|
Protein arginine N-methyltransferase 10
|
Xenopus
|
MAGQAASKRRLISRSLQSADICLQHQDYGTAYAHLLLVLTLAPEQKEALKEMFQYSLFKWAEELYALNRSQDLFNCYEQALELFPIDDVICNSMGEHLFRLGFRDEAAGYFYKALKLNPSSAEAKENFYRVANWLIERWHFIMLNDTKRNLMYRAAIQNAIQNGCKTVLDIGTGTGILSMFAKKAGAPFVYACELSKTMYELACEIVTANQMDGHIKLLHMKSHDIQIPEHIPERVSLVVTETVDAGLFGEGIVETLIHAWKNLLLQPKPKDGRVEAYGKVIPSSAVIYGMAVECPEIRRHYSVGVTEVAGIKLGDAVKFCSPIHSSHGPDDVTEPYTTEKMSRVPGGYKALSQPFQVMTVDFNSLQALEYIASGKSNRISVPVYQQGQFDCFITWFALQLDNEHSLSTEPSEETCWEQAVFPVQKLPDEGCLVNTGDTIVVDVSCPDCYLRLDLSTIVLSESSCDQTENMVMGNETDICDALANLHTTTNKGNMQELCILEPGEIALLNNAVYHESFMAAISKVIGSLELKESCSVVRNSQEQDVNFAQPVSEDRLHVLDVSEGFSILPLIAAKLGKVKAFSSVEKEQHRVALEKLSVINDLNNNESLEFCLSQLETDDGAAQKPKSDKMWSIIILDVIETCGLIRQDLLEKAAIARCLLEPGGKIFPHAVVMQGMLIESKTLLHEGSVQGNEPTLGFLIAPFINRFKVPAHVFLNLSTVPCIPLSEQFELLRLDLMNPCSNNQSSSVMRIKVNICRSGQVTAVTFWYHIHIDEAISLDTSSEASHWKQAAYVLETPTCVLEGEELLLEVQFQNSSMSMKLTRPLQ
|
Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA).
|
A0JMU5
|
P9WH04
|
DEAD_MYCTO
|
Cold-shock DEAD box protein A
|
Mycobacterium tuberculosis complex
|
MAFPEYSPAASAATFADLQIHPRVLRAIGDVGYESPTAIQAATIPALMAGSDVVGLAQTGTGKTAAFAIPMLSKIDITSKVPQALVLVPTRELALQVAEAFGRYGAYLSQLNVLPIYGGSSYAVQLAGLRRGAQVVVGTPGRMIDHLERATLDLSRVDFLVLDEADEMLTMGFADDVERILSETPEYKQVALFSATMPPAIRKLSAKYLHDPFEVTCKAKTAVAENISQSYIQVARKMDALTRVLEVEPFEAMIVFVRTKQATEEIAEKLRARGFSAAAISGDVPQAQRERTITALRDGDIDILVATDVAARGLDVERISHVLNYDIPHDTESYVHRIGRTGRAGRSGAALIFVSPRELHLLKAIEKATRQTLTEAQLPTVEDVNTQRVAKFADSITNALGGPGIELFRRLVEEYEREHDVPMADIAAALAVQCRGGEAFLMAPDPPLSRRNRDQRRDRPQRPKRRPDLTTYRVAVGKRHKIGPGAIVGAIANEGGLHRSDFGQIRIGPDFSLVELPAKLPRATLKKLAQTRISGVLIDLRPYRPPDAARRHNGGKPRRKHVG
|
DEAD-box RNA helicase involved in various cellular processes at low temperature, including ribosome biogenesis, mRNA degradation and translation initiation.
|
P9WH04
|
Q9QYU2
|
EFTS_RAT
|
2A3-2
|
Rattus
|
MSLLRSLRFFPVACTGRSARAVLLQPSQPWHTLHAGPSLSSSASSKELLMKLRRTTGYSFVNCKKALETCGGDLKQAEAWLHKQAQKEGWSKAAKLHGRKTKEGLIGLLQEENTAVLVEVNCETDFVSRNVKFQQLVQQVALGTMAHCQNLTDQLSTYSKGFLNSSELSELAAGPDGEGSLKDQLALAIGTLGENMSLKRAAWVKVPSGFYVGSYVHGEMQSPSLQNLVLGKYGALVICQTPEQITNLEEVGRRLGQHVVGMAPLSVGSLDDEPGGETETRMLPQPYLLDPSITLGQYVQPQGVTVVDFVRFECGEGEQVAEAE
|
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.
|
Q9QYU2
|
Q46GY9
|
HIS6_PROMT
|
ImGP synthase subunit HisF
|
Prochlorococcus
|
MVALRLIPCLDVSNGRVVKGVNFVGLRDAGDPVELGCRYSKAGADELVFLDITATYEKRSTLVDMVRRTSESVTIPFTVGGGISSLNGINELLRAGADKVSLNSSAVKDPSLISKGANRFGSQCIVVAIDAKKNKNIPNKWDVYVSGGRNNTGLDAIEWAEKVFEMGAGEILLTSMDGDGTQNGYDIELTKCIADKVPIPVIASGGAGCLRHIKEAFTLGKSSAALLASLLHDGQLTIREIKEYLIKENLPIRPIE
|
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
|
Q46GY9
|
Q2QLA2
|
CTTB2_HORSE
|
Cortactin-binding protein 2
|
Equus
|
MATDGASCEPDFSRSPEDAAGATAEAAKKEFDVDTLSKSELLMLLSVMEGELEARDLVIEALRARRKEVFIQERYGRFNLNDPFLALQRDYEAGAGDKEKKPVCTNPLSILEAVMAHCRKMQERMSTQLAAAESRQKKLEMEKLQLQALEQEHKKLASRLEEERGKNKHVVLMLVKECKQLSSKVIEEAQKLEEVMAKLEEEKKKTSALEEELSAEKRRSTEMEAQMEKQLSEFDTEREQLRAKLHREEAHTTDLKEEIDKMKKMIEQLKRGNDNKPSLSLPRKTKDRRLVSISVGTEGPMTRSVACQTDPVIESSDHVKKLPLTMPVKPSTGSPLVSANAKGNVCTNAALVRPGIDRQASHGDLIGSSLPTVPPPSANRIEENGPSTGSTADLTSSTPPLPNNAAPPTVQTPGVAPQSYSQASPMHSLHSPCANASLHPGLNPRIQAARFRFQGNANDPDQNGNTTQSPPSRDVSPTSRENLVAKQLARNTVTQALSRFTSPQAGAPPRPGVSPTGDVGTYPPVGRTSLKTPGVARVDRGNPPPIPPKKPGLSQTPSPPHPQLKVIMDSSRASNAGAKVDNKTVASPPSSLPQGNRVINEENLPKSSSPQLPPKPSIDLTVAPAGCAVSALATSQVGAWPAETPGLNQPACSESSLVIPTTIAFSSSINPVSASSCRAGASDSLLVTASGWSPSLTPLLMSGGPAPLAGRPTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGHSALYSAAKNGHTDCVRLLLNAEAQVDAADKNGFTPLCAAAAQGHFKCVQLLIAYDANINHAADGGQTPLYLACKNGNKECIKLLLEAGSDRSIKTRDGWTPVHAAVDTGNVDSLKLLMYHRAPAHGSSLHKEEPESSIFDLDRQGEESPEGTFKPVVPADLINQADREGWTAAHIAASKGFKNCLEILCRHGGLEPERRDKCSRTAHDVATDDCKHLLENLNALKIPLRISVGEIQPGNYGSDDFECENTICALNIRKQTSWDDFSKAVTQALTNHFQAISSDGWWSLEDMKFNNTTDSSIGLGASSVRSITLGNVPWSAGQSFTQSPWDFMRKNKAEQITVLLSGPQEGCLSSVTYTSMIPLQMLQNYLRLVEQYHNVIFHGPEGSLQDYIAHQLALCMKHRQMAAGFSCEIVRAEVDAGFSKEQLVDLFISSACLIPVKQSPVKKKIIIILENLERSSLSELLGDFLAPLENRCPESPCTFQKGNGTAECYYFHENCFLMGTIAKACLQGSDLLVQQHFRWVQLRWDGEPMQGLLQRFLRRKVVNKFRGQVPSPCDPVCKTVDWALAVWRQLNSCLARLGTPEALLGPKYFLSCPVIPGHAQATVKWMSKLWNAVIAPRVQDAILSRASVKRQPGLGQTIAKKHPSQGQQAVVKAALSILLNKAVLHGCPLPRAELDQHTADFKGGSFPLSLVSSYNSCSKKKGESGAWRKVSTSPRKKSSRFSSPTWNKPDLSEEGIKNKTISQLNCNRNASLSKQKSFENDLSLTLSLDQRFSLGSDDEADLVKELQSMCSSKSESDISKIADSRDDLRRFDSPGNNPAFSATVNNPRMPVSQKEVSPLSSHQTTECSNSQSKTELGVSRVKSFLPVPRSKVTPCSQNTKRSSSSSNTRQIEINNNSKEEIWNLRKNEQVEKPNK
|
Regulates the dendritic spine distribution of CTTN/cortactin in hippocampal neurons, thus controls dendritic spinogenesis and dendritic spine maintenance.
|
Q2QLA2
|
Q8WNU8
|
NEK11_MACFA
|
Never in mitosis A-related kinase 11
|
Macaca
|
MLKFQEAAKCVSGSTAISTYPKTLIARRYVLQQKLGSGSFGTVYLVSDKKAKRGEELKVLKEISVGELNPNETVQANLEAQLLSKLDHPAIVKFHASFVEQDNFCIITEYCEGRDLDYKIQEYKEAGKIFPDNQIIEWFIQLLLGVDYMHERRILHRDLKSKNIFLKNNLLKIGDFGVSRLLMGSCDLATTLTGTPHYMSPEALKHQGYDTKSDIWSLACILYEMCCMNHAFAGSNFLSIVLKIVEGDTPSLPERYPKELNTIMESMLNKNPSLRPSAIEILKIPYIDEQLQHLMCRHSEMTLEDKNLDCQKEAARLINAMQKRIHLQTLRALSEVQKMTPRERMRLRKLQAADERARKLKKIVEEKYEENSKRMQELRSRNFQQLSVDVLHEKTHLIGMEEKEEQPEGRPSCSPQDEDEERWQDREEEFDEPTLENLSEPQPIPSMDLRKLESIVEDATSDLGYHEIPEDPLVAEEYYADAFDSYCEESDEEEEEIVLAGPEKEIKNEGSQPTYRTNQQDSDIEALARCLENVLGCTSLDTKTIPSMAADVSPGPTIFNSVMARTKMKRMRESAMQKLGTEVFEEVYNYLKRARHQNASEAEIRERLEKVVPRASDCFEVDQLLYFEEQLLITMGK
|
Protein kinase which plays an important role in the G2/M checkpoint response to DNA damage. Controls degradation of CDC25A by directly phosphorylating it on residues whose phosphorylation is required for BTRC-mediated polyubiquitination and degradation.
|
Q8WNU8
|
C6DA40
|
NUOH_PECCP
|
NDH-1 subunit H
|
Pectobacterium
|
MSWLTPELTEILITVGKAIVILLVVVTCGAFMSMGERRLLGLFQGRYGPNRVGWGGSLQLVADMIKMFFKEDWVPNFTDKVIFTLAPMIAFTSMLIAFAIVPITPTWGVADLNIGILFFLMMAGLAVYAVLFAGWASNNKYSLLGAVRASAQTVSYEVFIGLSLMGVVAQAGSFNMRDIVDSQEHLWNVIPQFFGFITFAIAGVAVCHRHPFDQPEAEQEIADGYHIEYSGMKFGLFFVGEYIGIVTVSALMVTLFFGGWHGPILPPFVWFALKTGFFMMMFILIRASLPRPRYDQVMSFGWKVCLPITLLNLLATAAVILYNA
|
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. This subunit may bind ubiquinone.
|
C6DA40
|
Q5R6X6
|
PYRD_PONAB
|
Dihydroorotate oxidase
|
Pongo
|
MAWRHLKKRAQDAVVILGGGGLLFASYLMATGDERFYAEHLMPTLQGLLDPESAHRLAVRFTSLGLLPRARFQDSDMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKMGFGFVEIGSVTPKPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSVVEHRLRARQQKQAKLTEDGLPLGVNLGKNKTSVDAAEDYAEGVRVLGPLADCLVVNVSSPNTAGLRNLQGKAELRRLLTKVLQERDGLRGVHRPAVLVKIAPDLTSQDKEDIASVVKELGIDGLIVTNTTVSRPAGLQGALRSETGGLSGKPPRDLSTETIREMYALTQGRVPIIGVGGVSSGQDALEKIRAGASLVQLYTALTFWGPPVVGKVKRELEALLKEQGFCRVTDAIGADHRR
|
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. Required for UMP biosynthesis via de novo pathway.
|
Q5R6X6
|
A0AIY0
|
QUEA_LISW6
|
Queuosine biosynthesis protein QueA
|
Listeria
|
MKVEDFDFDLPEELIAQTPLLDRTSSRLMVLDKKSGEIKDQHFTDILSYLNEGDALVLNDTRVLPARLHGTKDETGAHIEVLLLKQKEGNAWETLVKPAKRIRKGGTITFGNGALKATCLEELEHGGRILEFSYEGIFYEVLEQLGEMPLPPYIKEQLADQDRYQTVYAKENGSAAAPTAGLHFTEDLLAQISAKGVEIIFVTLHVGLGTFRPVDVEDTANHKMHSEFYRLTEDAANRINKIKATGGKVVAVGTTSIRTLETIASHNEGKLVAESGWTDIFISPGYTFQAVDALITNLHLPKSTLIMLVSALSNRTNILAAYNHAVEQQYRFFSFGDAMFIH
|
Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
|
A0AIY0
|
Q5WGS1
|
TRPB_ALKCK
|
Tryptophan synthase beta chain
|
Alkalihalobacillus
|
MQETIPDSRGRFGEFGGKYVPETLMSAIEELEAGLAKAMVDPAFIGELKADLAEYAGRETPLTFAKNISAKLGGANIYLKREDLVHTGAHKLNNAIGQGLLAKRMGKNKLVAETGAGQHGVATATVASRLGMECKVFMGVEDMKRQELNVFRMELLGAEVVPAETGSRTLKDATNEAIRYWVSHADDTFYLIGSVVGPHPYPKMVRNFQRVIGDEAKQQMAEKTGRLPDTIVACVGGGSNAIGMFYPFLDDEVELVGVEAAGRGLDTAEHAATISKGSKGIIHGSLTYLLQDESGQIKEPYSISAGLDYPGVGPEHAYLAAQKRVRYEAVTDKEALDALALLAKEEGIIPAIESAHALAKAFQMAKTMTPNQSVLVCLSGRGDKDMHTLQRVYKEGYDE
|
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
|
Q5WGS1
|
Q5PIB9
|
RSXC_SALPA
|
Rsx electron transport complex subunit C
|
Salmonella
|
MLKLFSAFRKDKIWDFDGGIHPPEMKSQSNGTPLRQVPLAPRFVIPLKQHIGAEGELCVSVGDRVLRGQALTRGRGRMLPVHAPTSGTVIAIAPHSTAHPSALAELSVIIDADGEDRWIEREGWSDYRAHSREALIERIHQYGVAGLGGAGFPTGVKLQGGGDKITTLIINAAECEPYITADDRLMQDCAAQIVEGIRILAHILQPREVLIGIEDNKPQAISMLRAVLADAHDISLRVIPTKYPSGGAKQLTQILTGKQVPHGGRSSDIGVLMQNVGTAYAVKRAVVDGEPITERVVTLTGEAISRPGNVWARLGTPVRHLLNDAGFCPSADQMVIMGGPLMGFTLPWLDVPVVKITNCLLAPSVTEMGAPQEEKSCIRCSACADACPADLLPQQLYWFSKGQQHDKATAHHIADCIECGACAWVCPSNIPLVQYFRQEKAEINAIRLEEKRAAEAKARFEARQARLEREKAARLARHKSAAVQPAAKDQDAIAAALARVKEKQAQATQPVVIQAGSLPDNSAVIAAREARKAQARAKQAAHPMADSAISGDDPRKAAVEAAIARAKARKQEQQAGSEPAEPVDPRKAAVEAAIARAKARKQEQQAGSEPAEPVDPRKAAVEAAIARAKARKQEQQAGSEPAEPVDPRKAAVEAAIARAKARKQEQQAGSEPAEPVDPRKAAVEAAIARAKARKQEQQTVSEPVEPADPRKAAVAAAIARVQAKKAAQQQVVNED
|
Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Required to maintain the reduced state of SoxR.
|
Q5PIB9
|
Q65JQ2
|
Y2321_BACLD
|
UPF0122 protein BLi01817/BL02321
|
Bacillus
|
MTLEKTTRMNYLFDFYQTLLTSKQKSYMSLYYLDDFSLGEIAEEYHVSRQAVYDNIKRTEAMLEQYEEKLLLFKKFQERKKIFEALRKLTDGQPEAESLIDALEKLD
|
Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein.
|
Q65JQ2
|
Q72E03
|
ATPG_DESVH
|
F-ATPase gamma subunit
|
Desulfovibrio
|
MPSLKDVKVKIAGVKKTKQITKAMNMVASAKLRGAQQRIERFRPYAEKFYGMLGDLASKADGSAHPLLEVRDEIKTCGIVLATSDRGLCGSFNANLISTALKLAKQKAAEGKTVKFYCVGKKGRDTIRKADFEVVTAIADQMGSFDFQLANKLGLEVINHYLTGELDEVVLVYGEFVSTAKQLPITLPILPIASEKKDEAEAAPSKEYIYEPAVEGLLAELLPRFIKVQIYRGLLDTSASEHAARMAAMDNATRSCDDMIGALTLLFNKTRQASITRDLMDIVGGAEALKG
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
|
Q72E03
|
A6VIA5
|
ARGC_METM7
|
N-acetyl-glutamate semialdehyde dehydrogenase
|
Methanococcus
|
MKTVSIIGGTGYTGSELLRLLSTHEKVEVLNVTSRKEAGKKLTDFHPQVRNLRNYNDLEFQNIAPEDIDTDIVFCATPHGASMAIVPILHEKGINIIDLSGDYRFEDIEMYESWYGLKHTGKIESAVYGLPELHREKIKKSKTIANPGCYPTGAILSMAPLVANDLVDERIIFDSKSGVSGAGVEASQTTHFPNVNENLGAYKITKHRHSPEIGKELEYLGNKKLKVSFTPHLLPVTRGILTTAHSYLKEDVSRADVIEIYEEFYDGEFFVRIFEEGMVSLTGVRGTNFCDIGGFEIDQHGRIVVVSAIDNLVKGASGQAIQNMNIIMGFDEKMGLSVGGMRP
|
Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
|
A6VIA5
|
B0U5X4
|
RS7_XYLFM
|
30S ribosomal protein S7
|
Xylella
|
MSRKGSTPQRNVLPDPKYGSETIARFINMVMKSGKKSVAEKIVYGAMNVIGEKNSNAIELLQKALDNVSPAVEVKSRRVGGATYQVPVEVRASRRMALAMRWLIDSSRKRGENSMPRKLAAELLDASESRGGAIKKREETHRMAEANKAFAHYRW
|
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA.
|
B0U5X4
|
O74258
|
ACT_OGAPD
|
Actin
|
Ogataea
|
MDGEDVAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGIMVGMGQKDSYVGDEAQSKRGILTLRYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPMNPKSNREKMTQILFETFNVPAFYVSIQAVLSLYSSGRTTGIVLDSGDGVTHVVPIYAGFSLPHAILRIDLAGRDLTDYLMKILSERGYTFSTTAEREIVRDIKEKLCYVALDFDQELQTSSQSSAIEKSYELPDGQVITIGNERFRAPEVLFHPGPLGLEAAGIDQTTYNSIIKCDVDVRKELYGNIVMSGGTTMFPGIAERMQKEITALAPSSMKVKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHHKCF
|
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
|
O74258
|
Q1H4P7
|
RL1_METFK
|
50S ribosomal protein L1
|
Methylobacillus
|
MANVSKRIKALRAKVDRNKVYPVTEALALVKETATAKFDESVDAVINLGIDARKSDQLVRGALVLPHGTGKTKRVAVFAQGAAAEAAKAAGADIVGFEDLAEQVKGGMLDFDVAIATPDAMRIVGALGQVLGPRGLMPNPKVGTVTPDVATAVKNAKAGQVQYRTDKGGIVHCTIGRASFEVDALKENLAALVDALNKAKPASSKGVYLKKVSVSSTMGAGVRVDQSNLA
|
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.
|
Q1H4P7
|
P38044
|
NRTB_SYNE7
|
Nitrate import permease protein NrtB
|
Synechococcus
|
MTVTLRPPSSVRRSAWVKNPKLKPFLPYVVCLPIFLAIWQVISAILGQDRLPGPINVVANTWMPYIVEPFFDNGGTSKGLGLQILISLQRVAIGYLLAACTGILVGGVLGMSKFLGKGLDPVIQVLRTVPPLAWFPISLMVFQDANTSAIFVIFITAIWPIIINTAVGINQIPDDYNNVARVLKLSKKDYILNILIPSTVPYVFAGLRIAVGLAWLAIVAAEMLKADGGIGYFIWDAYNAGGDGSSSQIILAIFYVGLVGLSLDRLVAWVGRLVSPVSR
|
Part of the ABC transporter complex NrtABCD involved in nitrate uptake . The complex is probably also involved in nitrite transport . Probably responsible for the translocation of the substrate across the membrane .
|
P38044
|
B3ENW0
|
TRPA_CHLPB
|
Tryptophan synthase alpha chain
|
Chlorobium
|
MAQNRVSRLMQEDRKFLIAYYMPEFPLPGSTLPVLEALQKSGVDIIELGMPYSDPIGDGPVIQDAAHTAIGNGVHIAGILDLVRKARAGEGCEKITVPLLLMGYCSPLIAYGGDCFLSDASEAGVDGLLIPDLPPEEAEDFLFRARGFGLSVIFFISPETPPERIGMIDGLSTDFSYCFAVNATTGTAKLAGADSERDIESYLRRVREHTKKKFVVGFGIKDRARVEKMWNLADGAVVGTALLQAIRNASTPEEVALMTAEFWKTLKS
|
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
|
B3ENW0
|
A5D113
|
RSMH_PELTS
|
rRNA (cytosine-N(4)-)-methyltransferase RsmH
|
Pelotomaculum
|
MEFIHRPVMLDEVLEGLNLKPGGVYVDCTVGGAGHGEAILKRTGAEGRLIGIDRDPEALAAAERRLVPYGKRVDLVRANFEDIGKVLERLGQTGVDGILFDLGVSSYQLDNPARGFSYKRDSLLDMRMDPERGPSARELVNTLTAEELARIIKDYGEERWAFRIAAFIVEERKRSPIETTGRLAEIIKKAIPAGARREGPHPARRTFQALRIAVNRELEVLGGALRSAVRVLRPGGRICVITYHSLEDRIVKETFRRLASPCTCPKEFPACVCGGKKEIKIVTARPVVPSAGEVEENPRARSAKLRIAEKL
|
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
|
A5D113
|
Q5K0D2
|
O19_CONST
|
Omega-conotoxin-like 9
|
Pionoconus
|
MKLTCMMIAAVLFLTTWTFVTADDSRYGLKNLFPKARHEMKNPEASKLNKREGCSSGGTFCGIHPGLCCSEFCFLWCITFID
|
Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels (Cav).
|
Q5K0D2
|
Q3U829
|
AP5Z1_MOUSE
|
Adaptor-related protein complex 5 zeta subunit
|
Mus
|
MFSAGAESLLHQAREIQDEELRRFCSRVTKLLQEAPGPATVDALQRLFLIVSATKYPRRLEKMCVDLLQTTLCLPASPEQLQVLCAAILREMSPFNDLALSCDHTPNTRQLSLVASVLLAQGDRKGEIRCVSQRIFKILENRQPEGPSVRPLLPILSKVIGLAPGILMEDQTNLLSKRLVDWLRYASIQQGLPYSGGFFSTPRTRQPGPITEVDGAVASDFFTVLSTGQHFTEDQWVNMQAFSMLRKWLLHSGPEDPCSPDADDKSELEGSTLSVLSAASTASRLLPPRERLREVAFEYCQRLLEQSNRRALRKGDSDLQKACLVEAVSVLDVLCRQDPSFLYRTLSCLKALHRRLGEDPGSERALVPLAQFFLNHGEAAAMDAEAVYGQLLRGLPSERFHSPTLAFEVIHFCTHNLALFDSHFLSLLRLSFPSLFKFLAWNSPPLTAEFVVLLPALVDAGTAVEMLHALLDLPCLTAALDLQLRSTQTPSERLLWDISLRVPSCLEAFQDPQFQGLFRHLLRTKASGSTERLTPLHQVLKPMASCARVTQCAEAVPVLLQAFFSAVTQTADGALINQLALLLLERSDSLYPVPQYEARVHGVLSSQLLVLCKLKPSLVVELSRELLEFVGSVSSIHSRASVFTCVVWAIGEYLSVTWDKRCTAEQINKFFEALEALLFEVTQSRPLADLPCCPPEVVTALMTTLTKLASRSQDLIPRVSLFLSKMRTLAQNPATSSVHSEEGAESIRTRASELLTLLKMPSVAQFVFTPPAGVCQPRYHRDTNVALPLALRTVSRLVEKEAGLLPG
|
As part of AP-5, a probable fifth adaptor protein complex it may be involved in endosomal transport.
|
Q3U829
|
P54530
|
PTB_BACSU
|
Phosphotransbutyrylase
|
Bacillus
|
MKLKDLIGKASIHKNKTIAVAHAEDEEVIRAVKLAAEHLSARFLLTGDSKKLNELTSSMQGHQVEIVHANTPEESAKLAVRAVHHKTADVLMKGNVPTSVLLKAVLNRQEGLRSASVLSHVAVFDIPDFDRLMFVTDSAMNIAPSLEELRQILQNAVHVAHAVGNNMPKAAALAAVETVNPKMEATVNAAALAQMYKRGQIKGCIVDGPLALDNAVSQIAAAQKKISGDVAGNADILLVPTIEAGNILYKSLIYFAKASVAAVITGAKAPIALTSRADSAENKLYSIALAICASEEYTH
|
Catalyzes the conversion of butyryl-CoA through butyryl phosphate to butyrate.
|
P54530
|
C9JSJ3
|
MEIOS_HUMAN
|
Basic helix-loop-helix and HMG box domain-containing protein 1
|
Homo
|
MFGSSRYLGSSEQPRANSLGPSDRTLVLCSLVEGEDKVNPSEPHGLRMEEKWLLKGKLRNQRNQNKLLSPNKKQRKNHTSKLQELALLLPIALKTGTKKLTKKEILVHVLQYIQYLQRNIDAAKALFKCHITTGEGGLAGLGQKPAWGPARRRRHSTPSSSPSSQKSCLQGACQKPRKKKLTQASESQTRTPKPRRSLALNKPEKLVAPSPDQKGSGTGGTTTPPRCPDSCGHPRPASSSPPGDRKGGQSQLTLLDLAEDTIHCDISSCWCQGSVQDDAPFPALLAQEDVARIHFLNKTQPHPRQKLVFYDSSEDVDKGSLDADPWLPAWTPENSPQGSPLFLGPPQIDVWSGTGHPSEILGLSPSLFSSPGKLLPDEILEDDMEYLTQAAFFEEVCLDLESSPSAYTQEAPQEKDTASKAPKDPPESHSLHRSSVSLDHCYLSLSGNSKAPSSSSSSSSSSSSSEDSDSEPLWKQREDMQANPVGTPGSSEEDEDTTWTPTRLASPLLAAEKKATKGQVARAPVKPKEKKKGPCPPQMKKKCVNGFIMFCRMNRKQYIRSCPGTASTAATKELAQLWRVMTQQERRPYCTKARRFSRQHNRIVKQDGSSSEAEDWETPKPFYQLLAEKALPLPPHLQ
|
Gatekeeper of meiotic initiation in both male and female germ cells. In complex with STRA8, directly activates the transcription of a subset of critical meiotic genes playing a central role in cell-cycle switching from mitosis to meiosis. Temporal expression of MEIOSIN is required for meiotic entry decision.
|
C9JSJ3
|
P52826
|
CACP_COLLI
|
Carnitine acetyltransferase
|
Columba
|
MDRKQKQAEKARPYGLLKPAALGKIPGRFQLHQEALPHLPVPPLQQTLDRYLLALQPIISEEELNHTQELVAEFRKPGGVGERLQKGLERRAKKTDNWLSDWWLKTAYLEYRLPVVVHSSPGVVLPKQDFQDRQGQLRFAAKLIEGILDFKTMIDNETLPVEYMGGKPLCMNQYYQILSSCRIPGPKRDSIVNYAKGKKQSRHITVVHNFQFFELDVYNSDGSPLTTDQLFIQLEKIWNTSLQTNKEPVGILTTNHRNSWAKAYNNLLKDKTNKESVRTIEKSICTICLDAPMPRVSDDIYKSPVAAQMLHGGGSRWNSGNRWFDKTLQFIIAEDGSCGLVYEHAPAEGPPIVALLDHIVEYTKKPELVRSPMIPLPMPKKLRFNITPEIKSDIEKAKQNLNIMVEDLDVIVLVFHQFGKNYPKSEKISPDAFIQLALQLAYYRMYGHSCATYESASLRMFRLGRTDTIRSTSIESHKFVQSMDSPDKSDQEKADLLRRATQAHKEYTNMAIQGNAIDRHLLGLKLQAIEDLVSIPELFMDTAYAVAMHFNLSTSQVPAKTDCVMCFGPVVPDGYGICYNPMGEHINFAISAFNSCADTNAARMAHYLEKALLDMRSLLQSAPKSKL
|
Catalyzes the reversible transfer of acyl groups from carnitine to coenzyme A (CoA) and regulates the acyl-CoA/CoA ratio. Also plays a crucial role in the transport of fatty acids for beta-oxidation. Responsible for the synthesis of short- and branched-chain acylcarnitines. Active towards some branched-chain amino acid oxidation pathway (BCAAO) intermediates. Trans-2-enoyl-CoAs and 2-methylacyl-CoAs are poor substrates.
|
P52826
|
Q5FFG4
|
FMT_EHRRG
|
Methionyl-tRNA formyltransferase
|
Ehrlichia
|
MRIIFMGSPEFSVVALSSILNNTEHKIVSVYTRVPKPAGRGKVLTKTPIHTVAEMHGLTVYTPKSLKRIEEQDRIKELNPDVIVVVAYGLIIPKEVLSIPKYGCINIHPSLLPRWRGAAPIHYAILHGDSQTGVTIMQMNEGWDEGDILLQKKLSIDEQDNIETLSNKLSNLGGAMLVEVLNNIDNLVPVAQNEDNATYTNKIEDFHIDINETAEVACRRIRALYPRAFVFFNGKRLRILQASYYYDDSISSLKPSSILNSGMHIKCKGNTILVPLVVQMEGKTLCSIKDFVCGYNVKDYSIT
|
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.
|
Q5FFG4
|
Q2W8R0
|
MAMH_MAGSA
|
Probable magnetosome permease MamH
|
Magnetospirillum
|
MSRVEAAAAEVKVRQHNALYLLSALCMVFMTLVVAIQPLFLRNVLNISFETAGAVNANVQVVTEVLDLFIFAYLGYLSDRIGRVRIIVAGFLVAAIGAVIAPLSPWIGGASIGALVVYYVSRVIMSAGSGAVWPQLSALAGDFSDDDTRARLMSNTAFMMAFGVTLVYAVLMQIPAHAGIAVTMLLTAAVSLAGAWLAGKFLVDVAPRTQETSVPWRAVWSLVKAEPRLRLAFASSLFARSDMVFVGLFLMLWFIYFADLIKVGQAEAAARAGILIGLMGAVVMLSIPVWRSFIEHFGRIQAVLLGMVLSALGFIMLGFIINPFDWFIVLPILLIASGQAGCFVAPQILTVDYAPRDLLGSVLGAFNVIGCIGIIFFVQVGGFLFDYVGPPAPFVFTGVGNLIISAYALRLLKREARDGGGDDAPGDDGVA
|
Required for correct biomineralization of the magnetosome; probably transports some form of iron. Partially functionally redundant with MamZ.
|
Q2W8R0
|
Q2SMM1
|
RLME_HAHCH
|
rRNA (uridine-2'-O-)-methyltransferase
|
Hahella
|
MGRSKSSSRWLNEHHSDVYVKKSKEDGFRSRASYKLIELDRQDKLLRPGMTVIDLGAAPGGWSQVVADVVGDQGKVVACDLLSMDSIAGVTFFQGDFTEDEMLDAILNEVNSRPVDLVISDMAPNMSGMKSVDIPKAMYLVELALDLACRVLKKNGCFVAKVFQGEGFDQILQESRGRFSSVNIRKPDASRARSREIYLVAKGFRG
|
Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
|
Q2SMM1
|
Q04PT9
|
RL4_LEPBJ
|
50S ribosomal protein L4
|
Leptospira
|
MKAQKYSKEGKLISEIELPSALFESKLSVASIYEAIKAENANLRSGNHATKTRSEVRGGGKKPWSQKGTGHARQGSTRAPHWVGGGTVHGPQKRDYSYKVSSKLKHKAVLSILNKKAQASAVKVIEDLDPKEYSTKSFDSIFKNMNLRNTGVIGFLVQGESDFVKKSVRNIPTVKYINSKRISCRDILYNRNLVITEAALNEMLTQYGATK
|
Forms part of the polypeptide exit tunnel.
|
Q04PT9
|
Q09488
|
SMA6_CAEEL
|
Serine/threonine-protein kinase receptor sma-6
|
Caenorhabditis
|
MNITFIFILIFGFFNTQKCSKDYDHFDDEDLALSIPKNAIGVPKEFRQQVLKEMKLRNRPNDILKNRCYCNYDQSICGNNMTCVKQDGAACYHAVEEVYNKAEKRMETLHKWGCATLERGSGASHLTCNSWRAAHHSPKSIGCCYEGNYCNKNLIPPAYVHHHKEKALQEKTDNPEDYDSPLENMTRGGKMFIMVFATVMSVFAVIGCIYLCITRAEEKSKARARAKTVSLKTESTYMESKSMLEDSGSGSGQAALIQRTVRQDLTIIKTIGQGRYGEVRKALYRGSYVAVKTFYTTDEDSWKNERDVYQTNMINHENILQFVAADIWSEEDSMTKMLLITDYHELGSLSDYLCREETLTTDEALRLIHSCICGIEHLHAAVHGTGSFRKPEIAHRDIKSKNIIVKRPNVCCIADLGLALRYQNDKILPEKFNVQVGTKRYMAPELISNKLNPKDFSQFKMADIYSMALVMWEVAIRVEVNTCEEVLTVDETSPDHSASSGIGESVSSSGNISRMHLQKTNVEGHSTSLKAKQHVPPFDGIVHNDPNFDEMNDVICVRRIRPPPDLAWKNVPALNELSKLMEDSWHSIPHFRHSALKLKKEMAELIKNPDRQNQSQRKVEFQQQDSGLVESATNQS
|
Serine/threonine-protein kinase receptor which binds TGF-beta-like ligands dbl-1 and perhaps daf-7 . Upon ligand binding, probably activates a TGF-beta-like signaling pathway .
|
Q09488
|
Q8CY26
|
TRMD_COREF
|
tRNA [GM37] methyltransferase
|
Corynebacterium
|
MNAVTSANNNTDNRRLRLDVVSIFPEYLDPLRHALLGKAIEDGYLEVGVHDLRDWATGGHKAVDDTPYGGGPGMVMKPEVWGPALDDVAAGRVAGWELESATPHRNVARHDELAGVDKHAYEGEDADLPLLLVPTPAGKPFTQADAQAWSNENHIVFACGRYEGIDQRVIEDARNRYRVREVSIGDYVLIGGEVAVLVIAEAVVRLIPGVLGNRRSHEEDSFSDGLLEGPSYTKPRTWRGLDVPEVLFSGNHARVDRWRRDQALLRTQRVRPELLDAVELTTEDRKVLGLD
|
Specifically methylates guanosine-37 in various tRNAs.
|
Q8CY26
|
P28559
|
PHEA_AGLNE
|
R-phycoerythrin alpha chain
|
Aglaothamnion
|
MKSVITTTISARDAAGRFPSRSDLESVQGNIQRSAARLEAAEKISAGHEGVVKEAGDACFAKYTYLKTSGEAGDSQDKVNKCYRDIDHYMRLINYSLVVGGTGPLDEWGIAGAREVYRALNLPASAYIAAFAYTRDRVCVPRDMSAQAAVEFIGALDYVNSLS
|
Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex.
|
P28559
|
Q1XDJ0
|
RR5_NEOYE
|
30S ribosomal protein S5, chloroplastic
|
Neopyropia
|
MANRKKQSKGKDKDSGWEERVVQVKRVTKVVKGGKKLSFRVILVIGNEQGQVGVGVGKASDVIGAVKKGVTDAKKHLVTVPLTKSNSIPHPINGISGAAKVILRPSAPGSGVIAGGSVRTVLELSGVQNILAKQLGSNNTLNNARAVLNGLTQLRTFSEAAKDRGVPIESLYST
|
With S4 and S12 plays an important role in translational accuracy.
|
Q1XDJ0
|
B7MWU3
|
HIS6_ECO81
|
ImGP synthase subunit HisF
|
Escherichia
|
MLAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRVVDKSWVSRVAEVIDIPFCVAGGIKSLEDAGKILSFGADKISINSPALADPTLITRLADRFGVQCIVVGIDTWYDAETGKYHVNQYTGDESRTRVTQWETLDWVQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVREVCHVPLIASGGAGTMEHFLEAFRDADVDGALAASVFHKQIINIGELKAYLATQGVEIRIC
|
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
|
B7MWU3
|
Q06J33
|
RR7_BIGNA
|
30S ribosomal protein S7, chloroplastic
|
Bigelowiella
|
MSRRKLSKKRIFKKDPFYNNELIQIIINRIMKKGNKALARKIIYRSLKDIELVTKQDPIKIVEQAVSNVTPFVEIRSRRLGGSTTQIPVFINNERGVTLAIRWLFQASKNKAGNKYSIIKRLSSEIVNASNGMGEAIKKRDEMHRMAEANKTIVKYNVL
|
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit.
|
Q06J33
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.