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
A4QDZ3
ARGR_CORGB
Arginine repressor
Corynebacterium
MSLGSTPSTPENLNPVTRTARQALILQILDKQKVTSQVQLSELLLDEGIDITQATLSRDLDELGARKVRPDGGRAYYAVGPVDSIAREDLRGPSEKLRRMLDELLVSTDHSGNIAMLRTPPGAAQYLASFIDRVGLKEVVGTIAGDDTVFVLARDPLTGKELGELLSGRTT
Regulates arginine biosynthesis genes.
A4QDZ3
A8AY29
HIS1_STRGC
ATP phosphoribosyltransferase
Streptococcus
MSQITIALTKGRIEEDTVKLLTQAGFDMSFMADKGRSLIFESPDGRFRFLLVKGPDVTTYVRHGVADLGIVGKDILFEHPTGYLELLDLNFGLCKFSLASVPSYDPHDHKRKRIATKYPTVATNYFNQKGEDVEIISIQGSVEISPVLGLADAIVDIVETGHTLSANGLLVFEDICRVSVRLIANQASLKNNPDIMPFVAKIESLVGRREVAFK
Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
A8AY29
A5CU80
RPOA_CLAM3
Transcriptase subunit alpha
Clavibacter
MLIAQRPTLTEESISEFRSRFVIEPLEPGFGYTLGNSLRRTLLSSIPGAAVTSIRIDGVLHEFSTVPGVKEDVTEIILNIKGLVVSSEHDEPITAYLRKQGAGQVTAADISAPAGVEIHNPELVIATLNEKAKFELELTIERGRGYVSATQNRSEFSEAGQIPVDSIYSPVLKVTYRVEATRAGERTDFDRLVVDVETKSAITPRDAIASAGRTLTELFGLARELNSAAEGIEIGPAPVDAVLSSELSMPIEDLDLSVRSYNCLKREGINNVSELVALSETQLMNIRNFGQKSVDEVKDKLVELGLSLKDAVPGFDGAHYYSYDEDETTTN
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
A5CU80
A0LEQ3
NUOI1_SYNFM
NDH-1 subunit I 1
Syntrophobacter
MGNLKEILEGGWSLVEGMRVTFRRLLRPVVTVQYPREVVTLSPAFRGHIELKSFADTGTHKCIACGTCERMCPSNVIKVQGTKAQPKGAKVATHYVIDFTRCSLCGICVESCPTGTLQYSTEYELAGESRWDGVIDLMQRFEARRPQSL
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.
A0LEQ3
B6JLW7
RIMO_HELP2
Ribosome maturation factor RimO
Helicobacter
MQIKENKQLCLISLGCSKNLVDSEVMLGKLYNYTLTNDAKSADVILINTCGFIESAKQESIQTILNAAKDKKRGAILIASGCLSERYKDEIKELIPEVDIFTGVGDYDKIDIMIAKKQNQFSEQVFLSEHYNARIITGSSVHAYVKISEGCNQKCSFCAIPSFKGKLQSRELNSILKEVENLALKGYKDMTFIAQDSSSFLYDKGQKDGLIQLISAIDKQQALKSARILYLYPSSTTLELIGAIESSPIFQNYFDMPIQHISDSMLKKMRRNSSQAHHLKLLDAMKQVKESFIRSTIIVGHPEENEGEFEELSAFLDEFQFDRLNIFAFSAEENTHAYSLEKVPKKTINARIKALNKIALKHQNHSFKALLNKPIKALVENKEGEYFYKARDLRWAPEVDGEILINDSALTTPLQPGHYTIVPSVFKDNILLAKVLSPF
Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12.
B6JLW7
B1JJ32
ARNT_YERPY
Undecaprenyl phosphate-alpha-L-Ara4N transferase
Yersinia
MKLLKDSGAALLALFFVLVYLLPVNSRLLWQPDETRYAEISREMLQRGDWVVPYFMDIRYFEKPVAGYWFNNISQWIFGDSNFAVRFGSIFSTALSAVLVYWLATLLWRNRSTSVLATLIYLSFLLVFGIGTYAVLDPMISLWLTAAMVSFYLTLKAENWQQKVGAYALLGVACGMGFMTKGFLALAVPVIAVLPIVIQQKRIKDLVVFGPIAIVCAVLLSLPWALAIAQREPDFWNYFFWVEHIQRFAEASAQHKSPIWYYLPILCIGVLPWLGLLPGALFKGWRERATKPELFFLLSWVVMPLLFFSVAKGKLPTYILPCMAPLSLLMAAYATDCANNIRMRALKINGVINLLFGVACALVIVVIGLGLVKDIVAYGPQENQKVWLGVLAFAGWGVTGFITLRNNARNWRWAAACPLLFILLVGYLIPQQVVDSKQPQNFIKNNFSELSSSRYVLTDSVGVAAGLAWELKRSDILMFSEKGELTYGLAYPDSQDNYISNDDFPTWLAQARKKGDVSLVVQLARNEALPAHLPSADKVNLMNRLALLWYQKTP
Catalyzes the transfer of the L-Ara4N moiety of the glycolipid undecaprenyl phosphate-alpha-L-Ara4N to lipid A. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides.
B1JJ32
A1TTE9
SECA_ACIAC
Protein translocase subunit SecA
Acidovorax
MASNFLTKLFGSRNDRLLKQYRKTVARINAMEPEYEKLSDDALRAKTVEFQGRVARGESLDDLLPEAFAVGREASKRVMKMRHFDVQLLGGMALHHGKISEMRTGEGKTLTATLPVYLNALGGKGVHVVTVNDYLANRDARWMGRLYNFLGLTVGINLPQMPREEKQAAYAADITYGTNNEYGFDYLRDNMVYEARDRVQRALNFAIVDEVDSILIDEARTPLIISGQAEDHTAMYIAMNKVVPLLVRQEGEADPRTGEGVTKPGDFTIDEKSHQVFLTEQGHETAERVLAAQGLIPEGASLYDPSHITLMHHLYAALRANHLYHRDQHYVVQNGEIVIVDEFTGRLMSGRRWSEGLHQAVEAKEGVEIQAENQTLASITFQNYFRLYSKLSGMTGTADTEAYEFQEIYGLETVVIPPNRPSKRDDQLDRVYKTTREKYEAAIQDIRECHERGQPVLVGTTSIENSEIIDDLLNKAGLPHQVLNAKQHAREADIVAQAGRAGMITIATNMAGRGTDIVLGGNIEKEVAAIEDDESLDEATKQARIAALREQWAADNEKVKALGGLRIIATERHESRRIDNQLRGRSGRQGDPGSSRFYLSLDDSLMRIFAGERVRAIMERLKMPDGEAIEAGIVTRSIESAQRKVEARNFDIRKQLLEYDDVANDQRKVIYQQRNEILDAADLSGVIAGMRESCLTDIVRQYVPEESVEEQWDLAGLEKALADEWQIRLPLQQEVESAQAITDGEILEKVVAAGNAAFQAKVDMVGPENFHQFQRAVLLQSFDSNWRDHLSALDYLRQGIHLRGYAQKQPKQEYKREAFELFRQLIDQVKNEVTRILLTVQVQSPSELDQAAEALESRAEQIANVTYTAPTETGEPETLPDPRTAGAGGDGLNLPEGVRIGRNDPCPCGSGKKYKQCHGKLA
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.
A1TTE9
Q9I2E2
AZOR2_PSEAE
FMN-dependent NADH-azoreductase 2
Pseudomonas
MKLLHIDSSILGDASASRQLSAELVQAWRQNEDGLDVTYRDLAADAVAHFSALTLAAGSTPAELRDAALKHEVAVGEEVLEEFLAADVVVIGAPMYNFTISSQLKAWIDRIAVAGKTFRYTENGPVGLAGDKKVVIVSTAGGVHAGQPTGAAHEGYLRTVLGFFGITDIEVVRAEGLAYGEEPRTQAIAAARRQIAGQFAAA
Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines . Preferred substrates are the large bis-azo dye Ponceau BS, amaranth and tropaeolin O .
Q9I2E2
Q5MNH9
LOLE1_EPIUN
Loline biosynthesis cluster 1 protein E
Epichloe
MTAASSPHPGVSAEDIEFYQANGYLRLPQEAHGLFDDLAKLQAWVAEISQWGLETGKWRHYYETTNGKHLLWGTEKLMEYHAPMRDLIAGEAPLTLLKSLTGKDMVVFKDEIGWKLPGGKGAVPHLDRPAYSMFAPEFIEIMIAVDAHTVENGCLQFVPGSHKEAVPISADGRIASAWLEGKEFIPMVLDPGDVLIFNESMAHRLDPNKTDQRRAAVFGTYHFDRSQPDLRDKFYAHRLIHSPPENAWVETVEAQT
Dioxygenase; part of the gene cluster that mediates the biosynthesis of loline alkaloids, potent insecticidal agents composed of a pyrrolizidine ring system and an uncommon ether bridge linking carbons 2 and 7 . Lolines are structurally differentiated by the various modifications of the L-amino group and include norloline, loline, N-methylloline, N-acetylloline, N-acetylnorloline, and N-formylloline . The first committed step is the condensation of O-acetyl-L-homoserine (derived from L-aspartic acid) and L-proline, probably catalyzed by the gamma-type pyridoxal 5'-phosphate(PLP)-dependent enzyme lolC, to give the diamino diacid, NACPP . Ensuing cyclization, decarboxylation, and acetylation steps yield 1-exo-acetamidopyrrolizidine (AcAP). LolO is required for installation of the ether bridge upon the pathway intermediate, 1-exo-acetamidopyrrolizidine (AcAP) . In sequential 2-oxoglutarate- and O(2)-consuming steps, lolO removes hydrogens from C2 and C7 of AcAP to form both carbon-oxygen bonds in N-acetylnorloline (NANL), the precursor to all other lolines . The enzymes lolD, lolE, lolF and lolT have also been proposed to be involved in the ether-bridge installation . Further processing of the exocyclic moiety of NANL by fungal N-acetamidase (LolN), methyltransferase (LolM), and cytochrome P450 (LolP) enzymes, with occasional involvement of a plant acetyltransferase, generates the other known lolines . LolN transforms NANL to norlonine which is monomethylated and dimethylated to respectively lonine and N-methyllonine (NML) by lolM . LolP catalyzes hydroxylation of the methyl group in N-methylloline (NML) and further oxygenation to N-formylloline (NFL) . A plant acetyltransferase is responsible for the acetylation of loline to form N-acetylloline (NAL) . LolA might interact with aspartate kinase to prevent feedback inhibition of its activity by these end products and thereby promote production of L-homoserine from L-aspartate .
Q5MNH9
Q8IUF8
RIOX2_HUMAN
Ribosomal oxygenase MINA
Homo
MPKKAKPTGSGKEEGPAPCKQMKLEAAGGPSALNFDSPSSLFESLISPIKTETFFKEFWEQKPLLIQRDDPALATYYGSLFKLTDLKSLCSRGMYYGRDVNVCRCVNGKKKVLNKDGKAHFLQLRKDFDQKRATIQFHQPQRFKDELWRIQEKLECYFGSLVGSNVYITPAGSQGLPPHYDDVEVFILQLEGEKHWRLYHPTVPLAREYSVEAEERIGRPVHEFMLKPGDLLYFPRGTIHQADTPAGLAHSTHVTISTYQNNSWGDFLLDTISGLVFDTAKEDVELRTGIPRQLLLQVESTTVATRRLSGFLRTLADRLEGTKELLSSDMKKDFIMHRLPPYSAGDGAELSTPGGKLPRLDSVVRLQFKDHIVLTVLPDQDQSDEAQEKMVYIYHSLKNSRETHMMGNEEETEFHGLRFPLSHLDALKQIWNSPAISVKDLKLTTDEEKESLVLSLWTECLIQVV
Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Is involved in the demethylation of trimethylated 'Lys-9' on histone H3 (H3K9me3), leading to an increase in ribosomal RNA expression. Also catalyzes the hydroxylation of 60S ribosomal protein L27a on 'His-39'. May play an important role in cell growth and survival. May be involved in ribosome biogenesis, most likely during the assembly process of pre-ribosomal particles.
Q8IUF8
Q7UUZ6
RSGA_RHOBA
Small ribosomal subunit biogenesis GTPase RsgA
Rhodopirellula
MSVDEDNLLQGRVLSVHGLQSKVLGDNGVLYACAVRQVLKSLSTSQRNVIVAGDRVWFRSESRDGVSLKSEADGMIERVEPRTGMISRTSRGRQHVLVSNIDAMLIIASAEQPGIKPALIDRMILTAHQCQIEPIVIINKVDLIDLVDLQPLIGVYSSLGYRVLPTSAETGQNVAYLRALLKDRQTALAGQSGVGKSSLLNAVQPGLGLAIGAVSSDNDKGKHTTTASQLIPLADGGAVFDTPGIRQFQLWDISAGEVAGLMPDLRPYVSGCRYPDCLHLAEDDCAVKTAVADARIDARRYDAYCHLLEEELM
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Helps release RbfA from mature subunits. May play a role in the assembly of ribosomal proteins into the subunit. Circularly permuted GTPase that catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S ribosomal subunit.
Q7UUZ6
Q96N19
G137A_HUMAN
Transmembrane 7 superfamily member 1-like 1 protein
Homo
MESNLSGLVPAAGLVPALPPAVTLGLTAAYTTLYALLFFSVYAQLWLVLLYGHKRLSYQTVFLALCLLWAALRTTLFSFYFRDTPRANRLGPLPFWLLYCCPVCLQFFTLTLMNLYFAQVVFKAKVKRRPEMSRGLLAVRGAFVGASLLFLLVNVLCAVLSHRRRAQPWALLLVRVLVSDSLFVICALSLAACLCLVARRAPSTSIYLEAKGTSVCQAAAMGGAMVLLYASRACYNLTALALAPQSRLDTFDYDWYNVSDQADLVNDLGNKGYLVFGLILFVWELLPTTLLVGFFRVHRPPQDLSTSHILNGQVFASRSYFFDRAGHCEDEGCSWEHSRGESTRCQDQAATTTVSTPPHRRDPPPSPTEYPGPSPPHPRPLCQVCLPLLAQDPGGRGYPLLWPAPCCSCHSELVPSP
May activate Wnt/beta-catenin signaling to modulate epithelial cell function.
Q96N19
B7GN04
RISB_BIFLS
6,7-dimethyl-8-ribityllumazine synthase
Bifidobacterium
MHTFEGDLVAENITIGIVVARFNEFITSKLLAGALDTLKRENVREQDIAVAWVPGAFEIPLIASRMAKSKRYDAIICLGAVIRGSTSHYDYVCNEVSKGIAQTSLDTGVPVLFGVLTTDSIEQAIERAGTKAGNKGSECAQGAIEMVNLIRSMDL
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
B7GN04
A8AP50
MUTH_CITK8
Methyl-directed mismatch repair protein
Citrobacter
MPGLRPLLSPPASEALLLAQAQQLSGYSLGELAALAGLVAPKDLKRDKGWIGVLLEIWLGASAGSKPEQDFAALGVELKTIPVDSLGHPLETTFVCVAPLTGNSGVTWETSHVRHKLKRVLWVPVEGDRSIPLADRRVGSPLLWSPNEEEDQQLRLDWEELMDMIVLGQVERITARHGEFLQLRPKAANAKALTEAIGAQGETILTLPRGFYLKKNFTRTLLARHFLLQG
Sequence-specific endonuclease that cleaves unmethylated GATC sequences. It is involved in DNA mismatch repair.
A8AP50
Q8Q0M2
TRUD_METMA
tRNA-uridine isomerase D
Methanosarcina
MEVPEIEKQIGINLYSTDTTGLGGQLRQEIEDFIVKEITNREEGEEGKYLIVELTKRDWDTHHLTRTLSRILQVSQKRISVAGTKDKRALTTQKISIFDTDASEIEKIHLKDIELKVLGRSRKSVELGDLWGNDFRITVRNIENSPEETEALLKKTTDEILAQGGVPNFFGIQRFGSVRPVTHLVGKAIVEGNFEKAALLYIAEPFPEEPEETKNARQFVKDTLDFKEGLKTYPLRLGHERAMMNHLIANPEDYSGSFRVLPQNLYRMFVHGYQSYIYNIILCRRIEAGIPLNRAVEGDIVCFRNEVGLPDSSKTEKVTSETVNAMNRLLKLGRAFITAPLPGYNTEFASGIPGEIENGVLKELGVSLEGFNIEKFPEMSSKGTRREVLLEVKPKFEAGEDELNPGKSKAVLEFMLPKGSYATTVLREYMKVNPLQMS
Could be responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
Q8Q0M2
Q0TNC3
ATPG_CLOP1
F-ATPase gamma subunit
Clostridium
MAGAGLLEIKRRIKSIKNTRKITKAMGLVATSKLRKARQKLTENNQYFSSLDEIARELIGSLNSNNNPLLKPNDNPKKLIILLASDSGLCGGFNGNTAAFVRDNYENNLENIEAVVVGKKGIHYVKKNKISTLAEYVDLGDTPNVGDASTIVNKAVKEFTDGNFGEVSLVYTKFFSPVKQEVVEEKLLPLDLTGEKGKVSFLIEPDEDEIIDSLVSSYLKGKFMNAMFNSKASEQSARMQAMDGATKNADDLLNSLDAKYNRIRQSIITQEISEIVGGAEAQK
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.
Q0TNC3
Q9BDS7
GPR15_MACFA
G-protein coupled receptor 15
Macaca
MDPEETSVYLDYYYATSPNPDIRETHSHVPYTSVFLPVFYTAVFLTGVLGNLVLMGALHFKPGSRRLIDIFIINLAASDFIFLVTLPLWVDKEASLGLWRTGSFLCKGSSYMISVNMHCSVFLLTCMSVDRYLAIVCPVVSRKFRRTDCAYVVCASIWFISCLLGLPTLLSRELTLIDDKPYCAEKKATPLKLIWSLVALIFTFFVPLLNIVTCYCCIARKLCAHYQQSGRHNKKLKKSIKIILIVVAAFLVSWLPFNTFKLLAIVSGLQERYFPSAMLQLGMEVSGPLAFANSCVNPFIYYIFDSYIRRAIVHCLCPCLKNYDFGSSTETSDSHLTKALSTFIHAEDFTRRRKRSVSL
Probable chemokine receptor. SIV-1 coreceptor.
Q9BDS7
Q9ATN1
NIP31_MAIZE
ZmNIP3;1
Zea
MEPGSTPPNGSAPATPGTPAPLFSSGGPRVDSLSYERKSMPRCKCLPLPAVEGWGVATHTCVVEIPAPDVSLTRKLGAEFVGTFILIFFATAAPIVNQKYGGAISPFGNAACAGLAVATVILSTGHISGAHLNPSLTIAFAALRHFPWLQVPAYVAVQALASVCAAFALKGVFHPFLSGGVTVPDATVSTAQAFFTEFIISFNLLFVVTAVATDTRAVGELAGIAVGAAVTLNILVAGPTTGGSMNPVRTLGPAVAAGNYRQLWIYLLAPTLGALAGASVYKAVKLRDENGETPRTQRSFRR
Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.
Q9ATN1
P53739
FPK1_YEAST
Flippase kinase 1
Saccharomyces
MAGHHHEHEQERDHEQEHEHDSLQRPTTGSERTRSISFSKLLTRSWKRNASSSNNMSVSSVNLYSDPENSRESDHNNSGSEGQSSRFSKLKSMFQSGNSSKNASAHNSSQSSLEGDSASSSSKLRYVKPMTSVANASPASPPLSPTIPETDVLQTPKMVHIDQHEHEREHSNCGSPIMLSSSSFSPTVARTGTGRRRSPSTPIMPSQNSNNSSSTSAIRPNNYRHHSGSQGFSSNNPFRERAGTVRSSNPYFAYQGLPTHAMSSHDLDEGFQPYANGSGIHFLSTPTSKTNSLTNTKNLSNLSLNEIKENEEVQEFNNEDFFFHDIPKDLSLKDTLNGSPSRGSSKSPTITQTFPSIIVGFDNEYEEDNNNDKHDEKEEQQTTTDNKTRNLSPTKQNGKATHPRIKIPLRRAASEPNGLQLASATSPTSSSARKTSGSSNINDKIPGQSVPPPNSFFPQEPSPKISDFPEPRRSRRLRTKSFSNKFQDIMVGPQSFEKIRLLGQGDVGKVFLVREKKTNRVYALKVLSKDEMIKRNKIKRVLTEQEILATSNHPFIVTLYHSFQSEDYLYLCMEYCMGGEFFRALQTRKTKCICEDDARFYASEVTAALEYLHLLGFIYRDLKPENILLHQSGHIMLSDFDLSIQAKDSKVPVVKGSAQSTLVDTKICSDGFRTNSFVGTEEYIAPEVIRGNGHTAAVDWWTLGILIYEMLFGFTPFKGDNTNETFTNILKNEVSFPNNNEISRTCKDLIKKLLTKNESKRLGCKMGAADVKKHPFFKKVQWSLLRNQEPPLIPVLSEDGYDFAKLSSNKKRQTSQDSHKHLDEQEKNMFEERVEYDDEVSEDDPFHDFNSMSLMEQDNNSMIYGNTNSYGKIAYTPNSNRSRSNSHRTFFKR
Flippase activator that phosphorylates DNF1 and DNF2 and which is involved in the generation of phospholipid asymmetry in membranes by the inward translocation of phospholipids and in the retrieval pathway from early endosomes to the trans-Golgi network (TGN). Phosphorylates also the N-terminal half of YPK1. Involved in pheromone-response.
P53739
P25338
MPO1_YEAST
Metabolism of phytosphingosine to odd-numbered fatty acids protein 1
Saccharomyces
MGEGLLDLRSQLGFYKFYHHNPKNVLIHSIFVPTILFSGSCMLHRVKIYQSISLTAVLSVLFSIFYCLLYLPTGLLAGVLLLLLNLALIDHRVDLTFKQELGLFTIGWIFQFVGHGVFEKRRPALIDNLVQSLVLAPYFIMFEFLFKLGFMPRLKATLEHDLEIKQRNLRMQRQ
Dioxygenase that catalyzes the alpha-oxidation of 2-hydroxy fatty acids in an iron-dependent manner . Involved in metabolism of phytosphingosine and is required for proper endoplasmic reticulum stress response .
P25338
Q96G04
EF2KT_HUMAN
eEF2-lysine methyltransferase
Homo
MAPEENAGTELLLQSFERRFLAARTLRSFPWQSLEAKLRDSSDSELLRDILHKTVKHPVCVKHPPSVKYARCFLSELIKKHEAVHTEPLDELYEALAETLMAKESTQGHRSYLLPSGGSVTLSESTAIISYGTTGLVTWDAALYLAEWAIENPAVFTNRTVLELGSGAGLTGLAICKMCRPRAYIFSDCHSRVLEQLRGNVLLNGLSLEADITAKLDSPRVTVAQLDWDVATVHQLSAFQPDVVIAADVLYCPEAIMSLVGVLRRLAACREHQRAPEVYVAFTVRNPETCQLFTTELGRAGIRWEVEPRHEQKLFPYEEHLEMAMLNLTL
Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on 'Lys-525'.
Q96G04
Q44141
ANRX_NOSS1
Putative HNH nuclease
Nostoc
MTQKRPYEHRKAQKQVKNLESYQCMVCWEVNSKANGHHLIPYSEGGSADIQNMMTLCPSCHTKYHKGELKIDIHRF
Putative P-450 reductase.
Q44141
Q9XIE2
AB36G_ARATH
Protein PENETRATION 3
Arabidopsis
MDYNPNLPPLGGGGVSMRRSISRSVSRASRNIEDIFSSGSRRTQSVNDDEEALKWAAIEKLPTYSRLRTTLMNAVVEDDVYGNQLMSKEVDVTKLDGEDRQKFIDMVFKVAEQDNERILTKLRNRIDRVGIKLPTVEVRYEHLTIKADCYTGNRSLPTLLNVVRNMGESALGMIGIQFAKKAQLTILKDISGVIKPGRMTLLLGPPSSGKTTLLLALAGKLDKSLQVSGDITYNGYQLDEFVPRKTSAYISQNDLHVGIMTVKETLDFSARCQGVGTRYDLLNELARREKDAGIFPEADVDLFMKASAAQGVKNSLVTDYTLKILGLDICKDTIVGDDMMRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTFQIVKCLQQIVHLNEATVLMSLLQPAPETFDLFDDIILVSEGQIVYQGPRDNILEFFESFGFKCPERKGTADFLQEVTSKKDQEQYWVNPNRPYHYIPVSEFASRYKSFHVGTKMSNELAVPFDKSRGHKAALVFDKYSVSKRELLKSCWDKEWLLMQRNAFFYVFKTVQIVIIAAITSTLFLRTEMNTRNEGDANLYIGALLFGMIINMFNGFAEMAMMVSRLPVFYKQRDLLFYPSWTFSLPTFLLGIPSSILESTAWMVVTYYSIGFAPDASRFFKQFLLVFLIQQMAASLFRLIASVCRTMMIANTGGALTLLLVFLLGGFLLPKGKIPDWWGWAYWVSPLTYAFNGLVVNEMFAPRWMNKMASSNSTIKLGTMVLNTWDVYHQKNWYWISVGALLCFTALFNILFTLALTYLNPLGKKAGLLPEEENEDADQGKDPMRRSLSTADGNRRGEVAMGRMSRDSAAEASGGAGNKKGMVLPFTPLAMSFDDVKYFVDMPGEMRDQGVTETRLQLLKGVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDVRISGFPKVQETFARISGYCEQTDIHSPQVTVRESLIFSAFLRLPKEVGKDEKMMFVDQVMELVELDSLRDSIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRAVRNTVDTGRTVVCTIHQPSIDIFEAFDELMLMKRGGQVIYAGPLGQNSHKVVEYFESFPGVSKIPEKYNPATWMLEASSLAAELKLSVDFAELYNQSALHQRNKALVKELSVPPAGASDLYFATQFSQNTWGQFKSCLWKQWWTYWRSPDYNLVRFIFTLATSLLIGTVFWQIGGNRSNAGDLTMVIGALYAAIIFVGINNCSTVQPMVAVERTVFYRERAAGMYSAMPYAISQVTCELPYVLIQTVYYSLIVYAMVGFEWKAEKFFWFVFVSYFSFLYWTYYGMMTVSLTPNQQVASIFASAFYGIFNLFSGFFIPRPKIPKWWIWYYWICPVAWTVYGLIVSQYGDVETRIQVLGGAPDLTVKQYIEDHYGFQSDFMGPVAAVLIAFTVFFAFIFAFCIRTLNFQTR
Together with ABCG37, regulates auxin homeostasis and responses by playing a dual role in coumarine (e.g. esculin) and in the auxin precursor indole 3-butyric acid (IBA) efflux transport, thus influencing cotyledons, roots and root hairs development . Mediates the transport (export into the apoplast) of distinct indole-type metabolites in distinct biological processes; a precursor of 4-O-beta-D-glucosyl-indol-3-yl formamide (4OGlcI3F), a pathogen-inducible tryptophan-derived compound (e.g. upon Blumeria graminis conidiospore inoculation), being a probable substrate in extracellular pathogen defense . Involved in the cellular detoxification of xenobiotics by promoting the excretion of some auxinic herbicides including 4-(2,4-dichlorophenoxy)butyric acid (2,4-DB) and other members of the phenoxyalkanoic acid family but not 2,4-dichlorophenoxyacetic acid (2,4-D) . Mediates thymidine exudation in the rhizosphere . May be a transporter of lignin precursors during tracheary element differentiation . Key factor that controls the extent of cell death in the defense response . Necessary for both callose deposition and glucosinolate activation in response to pathogens . As a central component of nonhost resistance (NHR), required for limiting invasion by nonadapted pathogens including powdery mildews (e.g. Blumeria graminis and Erysiphe pisi), root-penetrating pathogenic fungi (e.g. Fusarium oxysporum), Phakopsora pachyrhizi and Colletotrichum gloeosporioides (anthracnose fungi), probably by sensing Ca(2+) via interactions with calmodulins (e.g. CaM7) . Confers resistance to cadmium (Cd) and lead (Pb), probably as an efflux pump of Cd2+ or Cd conjugates, and possibly, of chemicals that mediate pathogen resistance. Promotes resistance to abiotic stresses (e.g. drought and salt stress) and favors general growth by preventing sodium accumulation in plants . Required for microbe-associated molecular patterns (MAMPs)- and salicylic acid (SA)-dependent hypersensitive cell death (HR), involving indole glucosinolate breakdown products (e.g. indole-3-acetonitrile), probably in a PEN2 myrosinase-dependent metabolic pathway, triggered by the recognition of effectors from incompatible pathogens including oomycetes and bacteria (e.g. AvrRpm1 and AvrRps4) and benzothiadiazole- (BTH), and leading to an induced protection against pathogens (e.g. Pseudomonas syringae pv. tomato DC3000, Golovinomyces orontii and Hyaloperonospora arabidopsidis) .
Q9XIE2
Q60Z52
CED4_CAEBR
Cell death protein 4
Caenorhabditis
MLCEIECRALNAAHTMLIQDFEPRDALTYLEGEKIFTEDHSDLISNMPTRLERIANFLRAYRRQASELAPLIDFFEYNNQNHLKDFLDEYLWFATHQPDKLRPVVLVPKFSRQMLDRKLLLGNVPKQMNCFSREFHVDRVIEKLDEMCDLESFFLFLHGRSGSGKSVIASQALSKSDQLIGINYDSVVWLKDSGTTPKATFDLFTDLLLMLKRARVVSDTDDSHNMPDFINRVLSRSEDDLLNFPSVEHVTSVVLKRMIANALIDRPNTLFVLDDVVQEDTIRWAQELRLRCLITTRDVEISNAASPECEFIEVTPLESYECFELLESYGMPVPAIERDEDILHKTIDLTSGNPAALMMIFKSCEPKTFEKMAQLNSKLETRGLSAIECITPYCYKSLSSSLQRCVEVLSDEDRSALAFAVIMPPGIDIPVKIWSCVIPVDICSNEEDQLDDEVADRLKRLSKRGALLSGKRSPVLTYKIDHVIHLFLKHVVDVQTIANGISILEQRLHELGNNNTPTPERHMPSKFRRTSAGDMFPKVEDSVIRPEDYSKFMQIHRTFYDSLKKFTSQ
Plays a major role in programmed cell death (PCD, apoptosis). egl-1 binds to and directly inhibits the activity of ced-9, releasing the cell death activator ced-4 from a ced-9/ced-4 containing protein complex and allowing ced-4 to induce caspase ced-3 autoproteolytic cleavage and activation. Also forms an holoenzyme with processed ced-3 enhancing ced-3 activity. Component of the egl-1, ced-9, ced-4 and ced-3 apoptotic signaling cascade required for the initiation of programmed cell death in cells fated to die during embryonic and postembryonic development. During oogenesis, required for germline apoptosis downstream of ced-9 and upstream of ced-3 but independently of egl-1. May regulate germline apoptosis in response to DNA damage, probably downstream of let-60/ras and mpk-1 pathway. Regulates CEP neuron apoptosis in response to high Al(3+) levels. During male tail morphogenesis, promotes apoptosis of the tail-spike cell. During larval development, required for the elimination of transient presynaptic components downstream of egl-1 and ced-9 and upstream of ced-3 apoptotic pathway. Together with ain-1, a component of the miRNA-induced-silencing complex (miRISC), and probably upstream of ced-3, regulates temporal cell fate patterning during larval development. May play a role in resistance to S.typhimurium-mediated infection.
Q60Z52
P16620
PTP69_DROME
Protein-tyrosine-phosphate phosphohydrolase
Sophophora
MALLYRRMSMLLNIILAYIFLCAICVQGSVKQEWAEIGKNVSLECASENEAVAWKLGNQTINKNHTRYKIRTEPLKSNDDGSENNDSQDFIKYKNVLALLDVNIKDSGNYTCTAQTGQNHSTEFQVRPYLPSKVLQSTPDRIKRKIKQDVMLYCLIEMYPQNETTNRNLKWLKDGSQFEFLDTFSSISKLNDTHLNFTLEFTEVYKKENGTYKCTVFDDTGLEITSKEITLFVMEVPQVSIDFAKAVGANKIYLNWTVNDGNDPIQKFFITLQEAGTPTFTYHKDFINGSHTSYILDHFKPNTTYFLRIVGKNSIGNGQPTQYPQGITTLSYDPIFIPKVETTGSTASTITIGWNPPPPDLIDYIQYYELIVSESGEVPKVIEEAIYQQNSRNLPYMFDKLKTATDYEFRVRACSDLTKTCGPWSENVNGTTMDGVATKPTNLSIQCHHDNVTRGNSIAINWDVPKTPNGKVVSYLIHLLGNPMSTVDREMWGPKIRRIDEPHHKTLYESVSPNTNYTVTVSAITRHKKNGEPATGSCLMPVSTPDAIGRTMWSKVNLDSKYVLKLYLPKISERNGPICCYRLYLVRINNDNKELPDPEKLNIATYQEVHSDNVTRSSAYIAEMISSKYFRPEIFLGDEKRFSENNDIIRDNDEICRKCLEGTPFLRKPEIIHIPPQGSLSNSDSELPILSEKDNLIKGANLTEHALKILESKLRDKRNAVTSDENPILSAVNPNVPLHDSSRDVFDGEIDINSNYTGFLEIIVRDRNNALMAYSKYFDIITPATEAEPIQSLNNMDYYLSIGVKAGAVLLGVILVFIVLWVFHHKKTKNELQGEDTLTLRDSLSRALFGRRNHNHSHFITSGNHKGFDAGPIHRLDLENAYKNRHKDTDYGFLREYEMLPNRFSDRTTKNSDLKENACKNRYPDIKAYDQTRVKLAVINGLQTTDYINANFVIGYKERKKFICAQGPMESTIDDFWRMIWEQHLEIIVMLTNLEEYNKAKCAKYWPEKVFDTKQFGDILVKFAQERKTGDYIERTLNVSKNKANVGEEEDRRQITQYHYLTWKDFMAPEHPHGIIKFIRQINSVYSLQRGPILVHCSAGVGRTGTLVALDSLIQQLEEEDSVSIYNTVCDLRHQRNFLVQSLKQYIFLYRALLDTGTFGNTDICIDTMASAIESLKRKPNEGKCKLEVEFEKLLATADEISKSCSVGENEENNMKNRSQEIIPYDRNRVILTPLPMRENSTYINASFIEGYDNSETFIIAQDPLENTIGDFWRMISEQSVTTLVMISEIGDGPRKCPRYWADDEVQYDHILVKYVHSESCPYYTRREFYVTNCKIDDTLKVTQFQYNGWPTVDGEVPEVCRGIIELVDQAYNHYKNNKNSGCRSPLTVHCSLGTDRSSIFVAMCILVQHLRLEKCVDICATTRKLRSQRTGLINSYAQYEFLHRAIINYSDLHHIAESTLD
Possible cell adhesion receptor.
P16620
B4T8M7
AROL_SALHS
Shikimate kinase 2
Salmonella
MMQPLYLVGPRGCGKTTIGMALAQATGFRFADTDRWLQSHVQMSVADIVEKEGWGGFRARETAALEAVSAPSTVVATGGGIILTEYNRRYMHRVGVVIYLCAPVSTLVNRLEAEPEADLRPTLTGKPLSEEVREVLEQRDALYRETAHYIIDATKTPAQVVSEIIAALPPSTQRLQGDVYT
Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
B4T8M7
A3M3C7
MTGA_ACIBT
Peptidoglycan glycosyltransferase MtgA
Acinetobacter calcoaceticus/baumannii complex
MKAFIVRVLLIFIGAILFIQLWIFSSLVWWRTHEVDTTMFMRIDYWSDTSEPIIHEWLDYDDISDNFKHAILAGEDAKFIHHHGFDWDGIRFALERNNEQGEVVAGGSTVSQQLAKNLFLYNKRSFIRKGQETVATWMMERMWSKRRILEVYMNSVEFGKNLYGVEAAAQYYYGKSAKNLTREQAAFLAALLPDPKYYQDHRNDRKLQYRKRVILRYMNSTQIPE
Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors.
A3M3C7
P36603
RIR2_SCHPO
Ribonucleotide reductase small subunit
Schizosaccharomyces
MGLEHLEEFSYPKEHGEEVEYDSEQGVRKIYVKSIKETFNFDNVSEEEKQEGGDYYLGKKEDELDEVVLRPNPHRFVLFPIKYHEIWQFYKKAEASFWTAEEIDLSKDLVDWDNKLNADERYFISTVLAYFAASDGIVNENLLERFSSEVQIPEARCVYGFQIMIENIHSETYSLLLDTYIREPKEKQRHFDAILTMGSIKAKAKWALRWINDEDSTYAIRLVAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELICRDEGLHTDFACLMFSHLKHRPGRKVVEAIIVEAVDIEKEYFTDALPVSLLGMNKDLMCQYIEFVADRLLVALGNDKYYNVTNPFDFMENISLAGKTNFFEKKVSDYQIAGVMSGTKRAEKDDHTFTIDEDF
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
P36603
A1SHJ0
ATPG_NOCSJ
F-ATPase gamma subunit
Nocardioides
MAVSLREYRARIKSTESMKKITRAMELIAASRIIKAQQRAQSAAPYARELTRAVSAVATYSNVDHPLTREPENSQRVAMLIVTSDRGLAGAYSSSVLKEAERLAEKLRGEGKTIDVYLCGRKGEAYHRFRNRPVVRSWTGFSDQPSYDAALEVGTTLIDAFLDEEGEHAVDEVHVVYTRFRSMLLQEPTAVRLLPLEVVEGEERPASDEVLPLYEFEPSAEAVLDNLLPQYVQSRIFFAFLQAAASELAARQKAMKSATDNADELIKKYTRIANQARQAGITQEISEIVGGVNALADAQAGSE
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.
A1SHJ0
Q6AC27
IOLG_LEIXX
Myo-inositol 2-dehydrogenase
Leifsonia
MTTTPDLRVGVGGAGQMGADHIQRITRVISGATVSAIVEPDAGRAAAAAAAPGSRAFASLDDALDASALEAVVIATPGQFHELVLVPALAAGLPVLCEKPLTPDSAEALRVLELEQTLDRPHIQLGFMRRFDDEYRALRELVVSGDAGELLFLRGVHRNPSVPESYTQSMLITDSVVHEFDVMPWLAGSPVASVEVKYPRRNDRAPERLREPILVLIELRNGVLVDVEMNVSVRFGYQVATEAVFQTGTARIGQPAGLQRWSDARFSIAEHTSFTTRFARAYDAQVQAWVDAVRDGSLVAGPNAWDGYLVALACEAGVRALSEPGPIAFAPAERPAFYA
Involved in the oxidation of myo-inositol (MI) to 2-keto-myo-inositol (2KMI or 2-inosose).
Q6AC27
P45499
FTSZ_KOCRD
Cell division protein FtsZ
Kocuria
MDSSTPQNYLAVIKVVGIGGGGVNAVNRMIEEGLRGVEFIAINTDAQALLMSDADVKLDVGRELTRGLGAGANPDVGRQAAEDHEEEIQEVLKGADMVFVTAGEGGGTGTGGAPVVARIARSLGALTIGVVTRPFTFEGRRRSNQAENGIETLRDEVDTLIVIPNDRLLSISDRNVSMLDAFKSADQVLLSGVSGITDLITTPGLINLDFADVKSVMQGAGSALMGIGSAQGEDRAVKAAELAIASPLLEASIDGAHGVLLSIQGGSDLGLFEINEAARLVQEVAHPEANIIFGAVIDDALGDQARVTVIAAGFDSVSQETNANNSSPAQRQAESTRAAFGGDASRPSGLGRSPQRGGNSYGAPAAGFGSRQGQGQDDDIPDDAGFDVDLPAEADAPSSSNTSARKDSLDFPDFLK
Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.
P45499
P63130
GAK7_HUMAN
HERV-K_1q22 provirus ancestral Gag polyprotein
Homo
MGQTKSKIKSKYASYLSFIKILLKRGGVKVSTKNLIKLFQIIEQFCPWFPEQGTLDLKDWKRIGKELKQAGRKGNIIPLTVWNDWAIIKAALEPFQTEKDSVSVSDALGSCIIDCNENTRKKSQKETEGLHCEYVAEPVMAQSTQNVDYNQLQEVIYPETLKLEGKGPELVGPSESKPRGTSHLPAGQVPVTLQPQKQVKENKTQPPVAYQYWPPAELQYRPPPESQYGYPGMPPAPQGRAPYPQPPTRRLNPTAPPSRQGSELHEIIDKSRKEGDTEAWQFPVTLEPMPPGEGAQEGEPPTVEARYKSFSIKMLKDMKEGVKQYGPNSPYMRTLLDSIAHGHRLIPYDWEILAKSSLSPSQFLQFKTWWIDGVQEQVRRNRAANPPVNIDADQLLGIGQNWSTISQQALMQNEAIEQVRAICLRAWEKIQDPGSTCPSFNTVRQGSKEPYPDFVARLQDVAQKSIADEKARKVIVELMAYENANPECQSAIKPLKGKVPAGSDVISEYVKACDGIGGAMHKAMLMAQAITGVVLGGQVRTFGGKCYNCGQIGHLKKNCPVLNKQNITIQATTTGREPPDLCPRCKKGKHWASQCRSKFDKNGQPLSGNEQRGQPQAPQQTGAFPIQPFVPQGFQEQQPPLSQVFQGISQLPQYNNCPPPQAAVQQ
The products of the Gag polyproteins of infectious retroviruses perform highly complex orchestrated tasks during the assembly, budding, maturation, and infection stages of the viral replication cycle. During viral assembly, the proteins form membrane associations and self-associations that ultimately result in budding of an immature virion from the infected cell. Gag precursors also function during viral assembly to selectively bind and package two plus strands of genomic RNA. Endogenous Gag proteins may have kept, lost or modified their original function during evolution.
P63130
A8LVH1
RECF_SALAI
DNA replication and repair protein RecF
Salinispora
MYVRRLELVDFRSYERVGVDLEPGANVLVGHNGVGKTNLIEALGYVATLDSHRVATDAPLVRMGAGAAVIRCAVVHEGRELLIELEIVPGRANRARLGRSPARRARDVLGALRLVLFAPEDLELVRGDPAERRRYLDDLLVLRQPRYAGVRADYERVVRQRNALLRTAYLARKTGGTRGGDLSTLAVWDDHLARHGAELLAGRLDLVAALAPHVTRAYDAVAAGTGAAGIAYRPSVELPTPTTDRADLTAALSAALAAGRSAEIERGTTLVGPHRDDLTLTLGPLPAKGYASHGESWSLALALRLAGYDLLRVDGIEPVLVLDDVFAELDTGRRDRLAQLVGDASQLLVTCAVEEDVPARLRGARFVVRGGEVHRA
The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP.
A8LVH1
P62665
RS5_THET2
30S ribosomal protein S5
Thermus
MPETDFEEKMILIRRTARMQAGGRRFRFGALVVVGDRQGRVGLGFGKAPEVPLAVQKAGYYARRNMVEVPLQNGTIPHEIEVEFGASKIVLKPAAPGTGVIAGAVPRAILELAGVTDILTKELGSRNPINIAYATMEALRQLRTKADVERLRKGEAHAQAQG
Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body.
P62665
B9L9P0
RUVA_NAUPA
Holliday junction ATP-dependent DNA helicase RuvA
Nautilia
MIAALRGNIFEKDGGKILLDVNNVIYELNVSMITFSSVNDKGLFYITEIIKENEYTLYGFADKNEKKLFDSLIKLNGVGPKVALAICSTYTPQTFMDIIANHDINALKKIPGIGPKSAKRILMEMGEFEVVFEEQNPVFNQALSALESLGFNKNDIVKALNGIKSDNLEETIKLALKKLSKDIK
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.
B9L9P0
Q31R08
LEPA_SYNE7
Ribosomal back-translocase LepA
Synechococcus
MTDVSVSKIRNFCIIAHIDHGKSTLADRLLQETGTVQAREMKEQFLDNMELERERGITIKLQAARMNYRAQDGEQYVLNLIDTPGHVDFSYEVSRSLQACEGALLVVDASQGVEAQTLANVYLALENDLEIIPVLNKIDLPGADPERVKREIEEVIGLDCSGAIEASAKSGIGIGEILESIVHLVPPPSDTTGEPLRALIFDSYYDPYRGVIVYFRVIDGTVRKGDRIRLMASGKEYEIDELGVLSPNQVQVEELHAGEVGYIAASIKAVADARVGDTITLARARATEPLPGYVEAKPMVFCGLFPTDSDRYPDLRDALEKLQLSDAALQYEPETSSAMGFGFRCGFLGLLHMEIVQERLEREYNLDLITTAPSVVYQVTTLDGEVLRVDNPSKLPPPQQREKIEEPYVKVEIITPENYVGALMDLCQTRRGIFIDMKYLTQERTTLIYEMPLAEVVTDFFDQMKSRTKGYASMEYSLIGYREGELVRMDILINSEPVDPLATIVHRDKAYYVGKALVEKLKELIPRHQFKIPLQAAIGSRVIASESIPALRKDVLAKCYGGDISRKKKLLQKQAKGKKRMKAIGTVDVPQEAFMAVLKLDREG
Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.
Q31R08
A0QKZ0
Y4444_MYCA1
Putative S-adenosyl-L-methionine-dependent methyltransferase MAV_4444
Mycobacterium avium complex (MAC)
MTRTHDDEWDLASSVGATATMVAAGRAMATKDPRGLIDDPFAEPLVRAVGVDFFTKMMDGELDLDAIENATPVRIQSMVDGMAVRTKYFDDYFVDATDAGVRQVVILASGLDSRAYRLPWPAGTVVYEIDQPRVIEFKSNTLAEVGAEPTATRRTIPIDLRGDWPAALSAAGFDPAAPTAWLAEGLLIYLPPEAQDRLFDNITALSAPGSTIATEFVPGIVDFDAERVREMSGSFREHGVDIDMASLVYAGERNHVIDYLNGLGWRAEGVTRTELFHRHGIEVPAPEHDDPLGEIIFISATRTG
Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity.
A0QKZ0
Q11YU5
SECA_CYTH3
Protein translocase subunit SecA
Cytophaga
MLGILAKLFGTKSGRDIKKLQPLVERINEEFQKLHALDDNQLRAQTDKIKGIIDADLSGIDKQIKEHHDKIAANPDLSIDEKEVVFQAIDKLELERNKELEKVLEKVLPQAFAVVKDTARRWKENGKLTVTATPMDIELASRKKNVQIIGSTAEWSSKWLAAGTEVTWEMQHFDVQLIGGMVLHHGKISEMGTGEGKTLVATLPAYLNALARRGVHVVTVNDYLAKRDSEWMAPLFEFHGISVDCIDKYQPNSEERRKAYRADITYGTNNEFGFDYLRDNMATDKDDLVQRGHHYAMVDEVDSVLIDDARTPLIISGPVPKGDQHEFAELKPRIQRVLEEQKKLINTYLVEAKRYIAAGKEKEAGLELLRAHRGYPGYKPLIKQLSETGIKSILQKTENEYMAENNKRMPEVDLPLYFVIDEKHNQVDFTEKGVDFITGEQEDPTLFVLPDIGSELAKIEKDKSISDQERMEQTEKLLSDYSIKQERIHTLQQLLKAYTLFEKDTDYVIMDGKVKIVDEQTGRIMDGRRYSDGLHQALEAKENVRVEEATQTYATITLQNYFRMYHKLSGMTGTAETEEAEFQQIYNLDVVVVPTNRSIARLDEQDKVYKTTREKYNAVADEIVELTEKGRPVLVGTTSVDISELLSRMLKMRNIKHQVLNAKLHAKEADVVAEAGKPGTVTIATNMAGRGTDIKLTAEAKASGGLAIIGTERHESRRVDRQLRGRAGRQGDPGSSQFFVSLEDNLMRLFGSDRIAKFMDRMGYKEGEVIQHSMISNSIERAQKKVEENNFGQRKRLLEYDNVMNSQRVVIYKRRKNALYGERLKLDILNMIFDLCEDMVFGAYTTKNYDNFKLRSISVFGVIPDITEEVFNKATAETLVKSFYEEVLAHYEQKIKFVKEKTQPTFNELQLTRGETIENIVIPFTDGKRNINIIAPLKELAQSDSRALEQAIERYITLAVIDMHWKDHLREMDELKQSVQNAAYEQKDPLLVYKFEGFELFKKFVYTVNADIVSFLFKADIPKQDTVPVRELKQQPVQQPKYRETKDEAGSAFGGGNANQQVEEAVAPPKAEPLRSQKIANRNDKVSVQYMDGSVKRDIKYKAVEDDLLSNKCVLIEE
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 as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Q11YU5
Q9M8X1
GL12_ARATH
Putative germin-like protein subfamily 1 member 2
Arabidopsis
MKGLVQFLVAKIILLVLASTFVHCYDPNPLQDYCVATNGTNRVFVNGKFCKDPKLVTANDFFYSGLNIPGNTSNRLGASVTDVDVRRIPGLNTLGIAIARLDFAPGGQLPPHIHPRASQIILVLKGQLSVGFVSSNDYNYTLFSKILYPGDVFAFPIGLVQFHANTGKTHAVAIGVVGSQDPGVIPIGDAVFGSNPLIDPKLLAKAFALDVNIVRHVQRVFSSEGYIVK
May play a role in plant defense. Probably has no oxalate oxidase activity even if the active site is conserved.
Q9M8X1
P19531
AMYM_GEOSE
Glucan 1,4-alpha-maltohydrolase
Geobacillus
MKKKTLSLFVGLMLLIGLLFSGSLPYNPNAAEASSSASVKGDVIYQIIIDRFYDGDTTNNNPAKSYGLYDPTKSKWKMYWGGDLEGVRQKLPYLKQLGVTTIWLSPVLDNLDTLAGTDNTGYHGYWTRDFKQIEEHFGNWTTFDTLVNDAHQNGIKVIVDFVPNHSTPFKANDSTFAEGGALYNNGTYMGNYFDDATKGYFHHNGDISNWDDRYEAQWKNFTDPAGFSLADLSQENGTIAQYLTDAAVQLVAHGADGLRIDAVKHFNSGFSKSLADKLYQKKDIFLVGEWYGDDPGTANHLEKVRYANNSGVNVLDFDLNTVIRNVFGTFTQTMYDLNNMVNQTGNEYKYKENLITFIDNHDMSRFLSVNSNKANLHQALAFILTSRGTPSIYYGTEQYMAGGNDPYNRGMMPAFDTTTTAFKEVSTLAGLRRNNAAIQYGTTTQRWINNDVYIYERKFFNDVVLVAINRNTQSSYSISGLQTALPNGSYADYLSGLLGGNGISVSNGSVASFTLAPGAVSVWQYSTSASAPQIGSVAPNMGIPGNVVTIDGKGFGTTQGTVTFGGVTATVKSWTSNRIEVYVPNMAAGLTDVKVTAGGVSSNLYSYNILSGTQTSVVFTVKSAPPTNLGDKIYLTGNIPELGNWSTDTSGAVNNAQGPLLAPNYPDWFYVFSVPAGKTIQFKFFIKRADGTIQWENGSNHVATTPTGATGNITVTWQN
Converts starch into maltose.
P19531
O95625
ZBT11_HUMAN
Zinc finger and BTB domain-containing protein 11
Homo
MSSEESYRAILRYLTNEREPYAPGTEGNVKRKIRKAAACYVVRGGTLYYQRRQRHRKTFAELEVVLQPERRRDLIEAAHLGPGGTHHTRHQTWHYLSKTYWWRGILKQVKDYIKQCSKCQEKLDRSRPISDVSEMLEELGLDLESGEESNESEDDLSNFTSSPTTASKPAKKKPVSKHELVFVDTKGVVKRSSPKHCQAVLKQLNEQRLSNQFCDVTLLIEGEEYKAHKSVLSANSEYFRDLFIEKGAVSSHEAVVDLSGFCKASFLPLLEFAYTSVLSFDFCSMADVAILARHLFMSEVLEICESVHKLMEEKQLTVYKKGEVQTVASTQDLRVQNGGTAPPVASSEGTTTSLPTELGDCEIVLLVNGELPEAEQNGEVGRQPEPQVSSEAESALSSVGCIADSHPEMESVDLITKNNQTELETSNNRENNTVSNIHPKLSKENVISSSPEDSGMGNDISAEDICAEDIPKHRQKVDQPLKDQENLVASTAKTDFGPDDDTYRSRLRQRSVNEGAYIRLHKGMEKKLQKRKAVPKSAVQQVAQKLVQRGKKMKQPKRDAKENTEEASHKCGECGMVFQRRYALIMHKLKHERARDYKCPLCKKQFQYSASLRAHLIRHTRKDAPSSSSSNSTSNEASGTSSEKGRTKREFICSICGRTLPKLYSLRIHMLKHTGVKPHACQVCGKTFIYKHGLKLHQSLHQSQKQFQCELCVKSFVTKRSLQEHMSIHTGESKYLCSVCGKSFHRGSGLSKHFKKHQPKPEVRGYHCTQCEKSFFEARDLRQHMNKHLGVKPFQCQFCDKCYSWKKDWYSHVKSHSVTEPYRCNICGKEFYEKALFRRHVKKATHGKKGRAKQNLERVCEKCGRKFTQLREYRRHMNNHEGVKPFECLTCGVAWADARSLKRHVRTHTGERPYVCPVCSEAYIDARTLRKHMTKFHRDYVPCKIMLEKDTLQFHNQGTQVAHAVSILTAGMQEQESSGPQELETVVVTGETMEALEAVAATEEYPSVSTLSDQSIMQVVNYVLAQQQGQKLSEVAEAIQTVKVEVAHISGGE
May be involved in transcriptional regulation.
O95625
P92132
CATB2_GIAIN
Cathepsin B-like protease B2
Giardia
MKLFLLAAAAFSAPALTVSELNHIKSLNPRWKAGIPKRFEGLTKDEISSLLMPVSFLKNAKGAAPRGTFTDKDDVPESFDFREEYPHCIPEVVDQGGCGSCWAFSSVATFGDRRCVAGLDKKPVKYSPQYVVSCDHGDMACNGGWLPNVWKFLTKTGTTTDECVPYKSGSTTLRGTCPTKCADGSSKVHLATATSYKDYGLDIPAMMKALSTSGPLQVAFLVHSDFMYYESGVYQHTYGYMEGGHAVEMVGYGTDDDGVDYWIIKNSWGPDWGEDGYFRMIRGINDCSIEEQAYAGFFDE
Thiol protease which is required for parasite excystation and invasion of the proximal small intestine of the human host.
P92132
A6MMQ9
NDHI_DIOEL
NADH-plastoquinone oxidoreductase subunit I
Dioscorea
MFPMVTGFINYGQQTIRAARYIGQSFIITLSHTNRLPVTIQYPYEKSIASERFRGRIHFEFDKCIACEVCVRVCPIDLPVVDWRLEKNIKKKQLLNYSIDFGFCIFCGNCVEYCPTNCLSMTEEYELSTYDRHELNYNQIALGRLPMSVIGDYTIQTVLNWTQIKIDKNKLLDSRTITNY
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
A6MMQ9
Q52701
DNAK_RHOCA
Heat shock protein 70
Rhodobacter
MAKVIGIDLGTTNSCVAIMDGSQPRVIENSEGARTTPSIVAYTDNERLVGQPAKRQAVTNPTNTVFAVKRLIGRRTTDAEVEKDKKLVPYNIVDGGNGDAWVEVRGEKFSPAQVSAVILQKMKETAESYLGETVTQAVITVPAYFNDAQRQATKDAGKIAGLEVLRIINEPTAAALAYGLDKKDSKTIAVYDLGGGTFDISVLEIDDGLFEVKSTNGDTFLGGEDFDMRIVNYLADEFKKEHGVDLTKDKMALQRLKEAAEKAKIELSSASQTEINQPFISMNAATGVPLHMVMKLTRAKLESLVDDLIKASLKPCAAALKDAGVSKDEIDEVVLVGGMTRMPRVVEEVTKFFGKEPHKGVNPDEVVALGAAIQAGVLQGDVKDVVLLDVTPLSLGIETLGGVFTRLIDRNTTIPTKKSQIFSTAEDNQNAVTIRVFQGEREMAADNKMLGMFNLENIPPAPRGVPQIEVTFDIDANGIVSVKAKDKGTGKEQQITIQASGGLSDDDIEKMIKDAEANAEADKKRKELVEAKNTGESLLHSTRKSLEEHGDKVDGSTVEMIELACNALEESLKSEDPGKIKGAVQNLTDAAMKLGEAIYKAQASEAGPASDDEDGPRSVDDDIVDADFEDMGENKRK
Acts as a chaperone.
Q52701
P37998
CD2_HORSE
T-cell surface antigen CD2
Equus
MNLACKLLASFLLIFFFSSKGAVSKKNITILGALERDINLDIPAFQMSEHVEDIQWSKGKTKIAKFKNGSMTFQKDKTYEVLKNGTLKIKHLERIHEGTYKVDAYDSDGKNVLEETFHLSLLEMVSKPNISWSCTNTTLTCEVTKGTDFELKLYLNGRMIQKSPRKVIVYKRASNQIASFKCTANNTVSEESSSVVIRCTEKGLDIYLISGICGGGIILFVFLALLIFYISKRKKQNSRRNDEELEIRAHKVISEERGRKPHQIPGSTPLNPAASQPPPPPSHRPQAPGHRPQVPGHRPLPPGHRVQHQQQKRPAPTPGTQAHQQKGPPLPRPRVQPKPPRGATENS
CD2 interacts with lymphocyte function-associated antigen CD58 (LFA-3) to mediate adhesion between T-cells and other cell types. CD2 is implicated in the triggering of T-cells, the cytoplasmic domain is implicated in the signaling function.
P37998
Q6USK1
GERS_OCIBA
Geraniol synthase, chloroplastic
Ocimum
MSCARITVTLPYRSAKTSIQRGITHYPALIRPRFSACTPLASAMPLSSTPLINGDNSQRKNTRQHMEESSSKRREYLLEETTRKLQRNDTESVEKLKLIDNIQQLGIGYYFEDAINAVLRSPFSTGEEDLFTAALRFRLLRHNGIEISPEIFLKFKDERGKFDESDTLGLLSLYEASNLGVAGEEILEEAMEFAEARLRRSLSEPAAPLHGEVAQALDVPRHLRMARLEARRFIEQYGKQSDHDGDLLELAILDYNQVQAQHQSELTEIIRWWKELGLVDKLSFGRDRPLECFLWTVGLLPEPKYSSVRIELAKAISILLVIDDIFDTYGEMDDLILFTDAIRRWDLEAMEGLPEYMKICYMALYNTTNEVCYKVLRDTGRIVLLNLKSTWIDMIEGFMEEAKWFNGGSAPKLEEYIENGVSTAGAYMAFAHIFFLIGEGVTHQNSQLFTQKPYPKVFSAAGRILRLWDDLGTAKEEQERGDLASCVQLFMKEKSLTEEEARSRILEEIKGLWRDLNGELVYNKNLPLSIIKVALNMARASQVVYKHDQDTYFSSVDNYVDALFFTQ
Monoterpene synthase that catalyzes the formation of geraniol from geranyl diphosphate.
Q6USK1
Q8VXY9
UAH_ARATH
Ureidoglycolate amidohydrolase
Arabidopsis
MESLKRFLCSIALLLISLLLPSSLAQQQQHESIRTMEDFSGYPIHEPGQFGSINLASSLSVDAPGLQNQIDELSSFSDAPSPSVTRVLYTDKDVSARRYVKNLMALAGLTVREDAVGNIFGKWDGLEPNLPAVATGSHIDAIPYSGKYDGVVGVLGAIEAINVLKRSGFKPKRSLEIILFTSEEPTRFGISCLGSRLLAGSKELAEALKTTVVDGQNVSFIEAARSAGYAEDKDDDLSSVFLKKGSYFAFLELHIEQGPILEDEGLDIGVVTAIAAPASLKVEFEGNGGHAGAVLMPYRNDAGLAAAELALAVEKHVLESESIDTVGTVGILELHPGAINSIPSKSHLEIDTRDIDEARRNTVIKKIQESANTIAKKRKVKLSEFKIVNQDPPALSDKLVIKKMAEAATELNLSHKMMISRAYHDSLFMARISPMGMIFIPCYKGYSHKPEEYSSPEDMANGVKVLSLTLAKLSLD
Involved in the catabolism of purine nucleotides. Can use (S)-ureidoglycolate as substrate, but not (R)-ureidoglycolate or allantoate. The sequential activity of AAH, UGLYAH and UAH allows a complete purine breakdown without the intermediate generation of urea.
Q8VXY9
Q3J086
NTPPA_CERS4
Nucleotide pyrophosphatase
Cereibacter
MTLILGSASPRRRELLAQLGVTPDAILPPDIDEEPRRGELPRPYCARLAAEKAAAVAAGPEDVVLCADTTVALGRRILGKPADAGEAARFLVALGGRRHEVITAVAVRRGDRLWQREVVSQVKMKRLSDLELNAYLASGEWEGKAGGYAIQGLASAFIPWISGSFTGIVGLPLAETATLLAAAGVPLYRAAA
Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Q3J086
B7GYN0
RS12_ACIB3
30S ribosomal protein S12
Acinetobacter calcoaceticus/baumannii complex
MATTNQLIRKGRTTLVEKSKVPALKACPQRRGVCTRVYTTTPKKPNSAMRKVCRVRLTSGFEVSSYIGGEGHNLQEHSVVLIRGGRVKDLPGVRYHTVRGSLDCAGVKDRNQSRSKYGAKRPKK
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
B7GYN0
Q7N7A8
LPLT_PHOLL
Lysophospholipid transporter LplT
Photorhabdus
MNASSVVQPLLTRGMKAVLVSQFFSAFADNALLFAILAQLKAQFYPDWSQPILQIVFVLAYILLAPFVGQIADRFPKDRVMLFANSFKLLGAFTICLGYDPFLGYALVGVGAASYSPAKYGILVELTDGDRLVKANGLMEASTIIAILTGSVVGGFLSDWNLAIALLVCALMYGIAVVANFFIPRLSAVRRDKGWNLKKMLTDFASACCILWHNKGARFSLIGTSLFWGAGITLRFLLVLWVPVVLGISDNSTPTILNVMVAVGIIIGAGAAARFITLKTVHRCMPAGVLIGVMVVIFAVQHSIWASYVLLIILGIFGGLFIVPLNALLQESGRQTIGVGYAIAVQNLGENIAMLLMLGLYSLVIKIGVPVVTTGIGFGTLLALTITSLWIWNRFQRN
Catalyzes the facilitated diffusion of 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) into the cell.
Q7N7A8
Q7YN81
RR4_EIMTE
Apicoplast 30S ribosomal protein S4
Eimeria
MLRYLGPKLKKLKRLNIHMQPEFSTKYFILNTNKYNNKMILSFYLLELFEKQKLKFTFSLSEKIIKKYILFMHKYNYKKFNLINIIEIRLDNTIFNLGYSITIAQAKQLIIHGYFFVNFKLIKIPSFLLKKGDIITLSPKSYYIFKLCKKNLYKKYIKNSNIYDTIYICKNTLISIIYSILNIYNNNNYNNILIMKYYSY
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
Q7YN81
Q7VIN8
TIG_HELHP
PPIase
Helicobacter
MNFTTKRINSANAVINGSIALSKIEEKFEKVIKKIAKNIKIDGFRKGKVPTQVIKTRYKEQIDQDAQQEAIQELLTAALKELEIQPNSLIGNPMISQFNKLNDKIELEIKLGITPTLNLDNVEDYTPEVKLKTISKNLIDERLEEIAKNRAPLNEITQERTLQKDDTAQIDFEGFVDGKAFEGGKGENFNLAIGSNQFIPGFEDALIGMKNGEKRTIKVTFPEQYQAKHLAGKEASFDVTLHKILQKELPKIDDEFAKSIAGEESNLQSLKDMIKEQLEMEQKTEIYNKELKEKLVEILLKNISFDLPDLIVEQEMDILFRNALSQLKPEEFDKIKNNQDEAKKQRETHKDEARKSVQITFIMDALAKKYNIAINDNEVLQTIYYEAMMMGQDPKATLEHYQKNNLVPAIKMTMLEDRVLHYLLDKKFEESKANTNAQKDNQ
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Q7VIN8
P23005
CRGF_BOVIN
Gamma-crystallin IVA
Bos
MGKITFYEDRGFQGRHYECSSDHSNLQPYFSRCNSIRVDSGCWMLYEQPNFQGPQYFLRRGDYPDYQQWMGLNDSIRSCRLIPHTGSHRLRIYEREDYRGQMVEITEDCSSLHDRFHFSEIHSFNVLEGWWVLYEMTNYRGRQYLLRPGDYRRYHDWGATNARVGSLRRAVDFY
Crystallins are the dominant structural components of the vertebrate eye lens.
P23005
P69769
CM3K_CONRA
Conotoxin R3.1
Phasmoconus
MSKLGVLLTICLLLFPLTALPMDGDQPVDRLAERMQDNISSEQHTFFEKRLPSCCSLNLRLCPVPACKRNPCCTG
Kappa-conotoxins inhibits voltage-gated potassium channels (Kv). This synthetic toxin reversibly inhibits the insect potassium channel Shaker K+, the teleost homolog TSha1 and the mammalian Kv1.2/KCNA2 channel. Interacts with the pore region of the insect channel, in a state-dependent manner. Causes seizure when intracerebrovascularly injected into mice. Is also toxic when intrathecally injected into mice, but shows no visible effects by intraperitoneal injection. Shows protective effects on cardiac tissue when administered after an ischemic event.
P69769
A0A0C5DM37
CYADH_CATRO
Alcohol dehydrogenase 2
Catharanthus
MQIITCKAVVCWAAGEPPVVEEILVEPPRSGEVRIKILFASLCHTDVLACKGFPTPMFPRVLGHEGVGVVECVGEGVSELREGDVVIPTYLGECGECENCESGRTNLCRTYPLQAFTGLMPDGSSRMSSAKGGEMLYQFLSCSTWSEYTVIDANYAVKIDSRIPLPHASFLSCGFTTGFGATWKEAKLQEGSSTVAVLGLGAVGLGAVEGARVQGVTQIIGIDINDNKREKGEAFGMTHFINPKKDNNKSISELVKELTKGQGVDVCFECTGVPDLVNEALESTKIGTGNMIMLGAGTQKSMTINFVSLLGCRTFKYSVFGGVKVQSDLPLIIQKCLNKEIQKIEQLLTHQVQLEDINRAFELLKEPDCVKVLITL
May be a positive catalyzer of strictosidine production by assisting secologanin biosynthesis, thus being involved in monoterpene indole alkaloids accumulation.
A0A0C5DM37
Q8MCR6
MATK_LENCU
Intron maturase
Lens
MKESQVYLERARSRQQHFLYSLIFREYIYGLAYSHNLNRSLFVENVGYDNKYSLLIVKRLITRMYQQNHLIISANDSNKNSFWGYNNNYYSQIISEGFSIVVEIPFFLQLSSSLEEAEIIKYYKNFRSIHSIFPFLEDKFTYLNYVSDIRIPYPIHLEILVQILRYWVKDAPFFHLLRLFLCNWNSFITTKKKKSISTFSKINPRFFLFLYNFYVCEYESIFVFLRNQSSHLPLKSFRVFFERIFFYAKREHLVKLFAKDFLYTLTLTFFKDPNIHYVRYQGKCILASKNAPFLMDKWKHYFIHLWQCFFDVWSQPRTININPLSEHSFKLLGYFSNVRLNRSVVRSQMLQNTFLIEIVIKKIDIIVPILPLIRSLAKAKFCNVLGQPISKPVWADSSDFDIIDRFLRISRNLSHYYKGSSKKKSLYRIKYILRLSCIKTLACKHKSTVRAFLKRSGSEEFLQEFFTEEEEILSLIFPRDSSTLERLSRNRIWYLDILFSNDLVHDE
Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns.
Q8MCR6
B1LAP5
RIMP_THESQ
Ribosome maturation factor RimP
unclassified Thermotoga
MFEEMILEKVRKEAERIAEEQGLEIFDVQYRRESRGWILRIIIDNPMGYVSVRDCELFSREMERFLDREDLIEHSYTLEVSSPGLDRPLRGPRDYVRFTGKLAKIVTKDGKTFIGRIESFVDGTITISDGKKKYEINIDDVKRANLEVEF
Required for maturation of 30S ribosomal subunits.
B1LAP5
Q8YNP4
ANMK_NOSS1
AnhMurNAc kinase
Nostoc
MYSSQASAVPNRVVGLISGTSVDGIDAALVEITGTELDLKVELLAGKTYPYPADLRERILAVCAGEAISMLELAHMDDAIALAFAQAAQNIQIGYQPANLIGSHGQTVYHRPPKEAGVGKKNLGYTLQLGRGEMIAYLTGITTVSNFRVADIAVGGHGAPLVPRVDAFLLSHPHESRCIQNLGGIGNLAYIPARTDDWLSQICGWDTGPSNSLLDLAVERLTAGAKTYDEDGQWAASGTPCYPLVEKWLTHEYFHLSPPKSTGRELFGVAYLNQCFQDAEPYQLSPADMLATLTELTVASIVHSYRTFLPQMPQRVFLCGGGSRNLYLKQRLQLALETVPVLTTDEAGVSADFKEAIAFAVLAHWRQLAIPGNLPTATGAPHEVLLGEIHQG
Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.
Q8YNP4
Q96FC9
DDX11_HUMAN
Keratinocyte growth factor-regulated gene 2 protein
Homo
MANETQKVGAIHFPFPFTPYSIQEDFMAELYRVLEAGKIGIFESPTGTGKSLSLICGALSWLRDFEQKKREEEARLLETGTGPLHDEKDESLCLSSSCEGAAGTPRPAGEPAWVTQFVQKKEERDLVDRLKAEQARRKQREERLQQLQHRVQLKYAAKRLRQEEEERENLLRLSREMLETGPEAERLEQLESGEEELVLAEYESDEEKKVASRVDEDEDDLEEEHITKIYYCSRTHSQLAQFVHEVKKSPFGKDVRLVSLGSRQNLCVNEDVKSLGSVQLINDRCVDMQRSRHEKKKGAEEEKPKRRRQEKQAACPFYNHEQMGLLRDEALAEVKDMEQLLALGKEARACPYYGSRLAIPAAQLVVLPYQMLLHAATRQAAGIRLQDQVVIIDEAHNLIDTITGMHSVEVSGSQLCQAHSQLLQYVERYGKRLKAKNLMYLKQILYLLEKFVAVLGGNIKQNPNTQSLSQTGTELKTINDFLFQSQIDNINLFKVQRYCEKSMISRKLFGFTERYGAVFSSREQPKLAGFQQFLQSLQPRTTEALAAPADESQASTLRPASPLMHIQGFLAALTTANQDGRVILSRQGSLSQSTLKFLLLNPAVHFAQVVKECRAVVIAGGTMQPVSDFRQQLLACAGVEAERVVEFSCGHVIPPDNILPLVICSGISNQPLEFTFQKRELPQMMDEVGRILCNLCGVVPGGVVCFFPSYEYLRQVHAHWEKGGLLGRLAARKKIFQEPKSAHQVEQVLLAYSRCIQACGQERGQVTGALLLSVVGGKMSEGINFSDNLGRCVVMVGMPFPNIRSAELQEKMAYLDQTLSPRPGTPREGSGGEPVHEGRQPVHRQGHQAPEGFCQRSAPGPAICPAPCPGQAAGLDPSPCGGQSYLWPRHCCCAEVSPGEVGLFLMGNHTTAWRRALPLSCPLETVFVVGVVCGDPVTKVKPRRRVWSPECCQDPGTGVSSRRRKWGNPE
(Microbial infection) Required for bovine papillomavirus type 1 regulatory protein E2 loading onto mitotic chromosomes during DNA replication for the viral genome to be maintained and segregated.
Q96FC9
Q9LD95
SIGF_ARATH
RNA polymerase sigma factor sig6
Arabidopsis
MEATRNLVSSSPSFQTKTHLKSSYSSPSSVVMLHDQTTTPVVNSRHLNSLSRHFPASVLSQEPREESRPLSHALRDDRTSQLTLERRQFDELVSSREDEKFEQQLLHSTGLWNLLISPLTSETKLPAVVSPLADAELCDVVALAQKALSASKQAALLVDDTEANPSDNIKDSLSTSSSMSLPEKGNIVRSKRQLERRAKNRRAPKSNDVDDEGYVPQKTSAKKKYKQGADNDDALQLFLWGPETKQLLTAKEEAELISHIQHLLKLEKVKTKLESQNGCEPTIGEWAEAMGISSPVLKSDIHRGRSSREKLITANLRLVVHIAKQYQNRGLNFQDLLQEGSMGLMKSVEKFKPQSGCRFATYAYWWIRQSIRKSIFQNSRTIRLPENVYMLLGKVSEARKTCVQEGNYRPSKEELAGHVGVSTEKLDKLLYNTRTPLSMQQPIWSDQDTTFQEITPDSGIETPTMSVGKQLMRNHVRNLLNVLSPKERRIIKLRFGIDGGKQRSLSEIGEIYGLSKERVRQLESRALYRLKQNMNSHGLHAYADLLV
Sigma factors are initiation factors that promote the attachment of plastid-encoded RNA polymerase (PEP) to specific initiation sites and are then released. Regulates transcription in chloroplast in a DG1-dependent manner. Involved in light-dependent chloroplast development. Required during early plant development and primary leaf formation.
Q9LD95
Q7MT07
DEF_PORGI
Polypeptide deformylase
Porphyromonas
MLLPIYLYGHPVLRKVAEDITPDYPKLKELIANMTESMYHSDGIGLAAPQIGLPIRVLVIDADPLKEDYPECAGFKRVMINAHIEERGEDLCTEYEGCLSLPAIHEKVERPTSIRIRYVDEDFQPHEEVLQGFAARVVQHEYDHIDGKLFIDHISPIRKQLIKGKLQNIIKGKVRTSYRVVTAPTGKKR
Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
Q7MT07
O69469
RNC_MYCLE
Ribonuclease III
Mycobacterium
MTQPRQALLDAFGVDLPDELLSLALTHRSYAYEHGGLPTNERLEFLGDAVLSLTITDELFHRHPDRSEGDLAKLRASVVNTQALAYVARNLSDGGLGVYLLLGRGETNTGGADKSSILADGMESLLGAIYLHHGIEVARQVILRLFGTLLDAAPTLGAGLDWKTSLQELTAARGMGVPSYVVTSTGPDHDKEFTAVVVVMDTEYGSGIGHSKKEAEQKAASAAWKALDVLGGVGKTSV
Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
O69469
A0A172M470
RLR25_PLAVT
Secreted RxLR effector protein 25
Plasmopara
MRSWLLLLVGLSSYFALSTSVNRAKNSGSDFDLESRASTTNVNSILSKRKLRAPGGDTNTLKDSGKARREKKVWKLFCRVFLQLDDEKKCMFETNQVSSHQPEPRPALSFMPGPKPAHSLVPESKPVRSLMTGNAPVRSIATKLKLVLPRITETVKNPSKSQVVMLWLHKVAEFSRSEHGVNTMSYRTLYEWLSPSFSDAKLAKFFVGLREDEALRETAEKMLAYMLIKSTSTEAVGRAWLKSGEHPSRLFESMNFKEADFKDTVFLGWLKYASLYEKHYFSQSELTDYRRQLFFYRMYDYIKPMYSYEKTQGFLEYKFEGLTSIPGMQDFGQNLADIARRERKISFYLDSEFTPEALFNYLKVSDENLLTNVFQWLRYCRRYTMAYKYVPFDELEFLEEKLGEISLWIYQVYGKL
Effector that partially suppresses the tobacco programmed cell death induced by cell death-inducing proteins.
A0A172M470
Q9JWF3
THIC_NEIMA
Thiamine biosynthesis protein ThiC
Neisseria
MTTPKKTAKTSGNEARELADLSEDIGIRFKYPNSERVYLQGSRDDIRVPLREIRQDDTYTAQGAEANPPIPVYDTSGVYGDPAAHIDLKQGLPHIRTVWLDERGDTEILPKLSSEYGIERAHDPKTAHLRFNQITRPRRAKAGRNVTQLHYARQGIITPEMEFVAIRERLKLDELSQKPEYAKLLKQHAGQSFGANIPTHPDQITPEFVRREIAAGRAIIPANINHPELEPMIIGRNFRVKINGNLGNSAVTSSLTEEVEKMVWSLRWGADTIMDLSTGAHIHETREWIIRNAPVPIGTVPIYQALEKTGGIAEDLTWDLFRDTLIEQAEQGVDYFTIHAGVLLRYVPMTANRLTGIVSRGGSIMAKWCLAHHRENFLYTHFDEICEIMKAYDVSFSLGDGLRPGCIADANDESQFAELHTLGELTDKAWKHDVQVMIEGPGHVPLQRVKENMTEELQHCFEAPFYTLGPLVTDIAPGYDHITSGIGAANIGWYGTAMLCYVTPKEHLGLPDKEDVRTGIITYKLAAHAADLAKGWPGAQLRDNALSKARFEFRWRDQFRLSLDPERAESFHDETLPAEGAKIAHFCSMCGPKFCSMKITQEVRDYADKQKAQRQGMEEKAVEFVKKGAKIYS
Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
Q9JWF3
Q2FRU6
DADD_METHJ
S-adenosylhomocysteine deaminase
Methanospirillum
MADPKDISPCKNEDLFLKCRSTLITGVLLPDKTRSDIWYDETGTIRTCGPDIARNHRNEADIILDGSGFLAMPGLINTHTHAAMTLLRGYADDMHLQQWLSEKIWPLEAHLTGEHVYWGTKLACLEMIRSGTIAFNDMYFYMKDAARAVQESGIRAVLSHGIITFGDEAKMEAELKATEDLVHHVRSLNTSLITSAIAPHAPYTVPPQHLEVCADYSQKEKIIIHTHLAETKQEVDDCQKSYGMTPAALLDKTGCLTERTVAAHGCWLSEDDCRLLAERRVSVAHNPVSNMKLATGRAMPYHWLKDQGVNVCLGTDGCSSNNNLDMLEEMKTAALCQKFFWNSDTLLPAAEALSMGTSWGAKALGYQGGVIQEGMPADIVLISLSHPSMVPLHNPVSNIAYSAEGSVVDTVICQGKILMYNRYIPDEEKIIAGARESADDLLNRAGIMA
Catalyzes the deamination of three SAM-derived enzymatic products, namely 5'-deoxyadenosine, S-adenosyl-L-homocysteine, and 5'-methylthioadenosine, to produce the inosine analogs. Can also deaminate adenosine. The preferred substrate for this enzyme is 5'-deoxyadenosine, but all these substrates are efficiently deaminated. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. May also be involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.
Q2FRU6
Q4JB24
PSA_SULAC
Proteasome core protein PsmA
Sulfolobus
MALGPAAMGYDRAITIFSPDGSLYQVDYAFEAVKRGWTTLGVKTKSGVVLLAEKRKATQLLDVDGIEKIFMLDDHVGCTFAGLASDGRILIDYARSQALQHRLIYDEPISIEYLTKVISDVKQAYTQHGGVRPFGVALIVGGIDKGKQPKLLMTEPSGQFMPYYAVAIGQGGYTATEYLEKNYKEDLDIQSTILLALRALMATLKPGEKLNYSSVEIGYADVDSGTFKKLTTEERSDLLQKI
Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
Q4JB24
Q89B34
YIDC_BUCBP
Membrane protein YidC
Buchnera
MHLQRNFFILIFFFISFLLWKTWQQKEFSSDVHKIINKYENVNLVNNNINKLASNIIIKTDVLKIQVNLYGGDIEKAELLHFKSKLNSSQSLVLLDTNENFVYQAQCGITGKDGADNLQKHIRPLYIAKRKYYELSRHNKKIEVPLQWISKDGIIYKKIFVLKSGEYDVSVKYKINNITNKHLKVSMFGQLKQTINLPEDKNTYTNNFALQTFRGAAYSSDNDKYVKYSFDSIVNKEKKNIVVTHSGWVAMLQKYFATSWIPDNSYLNTMYIGSSGDNLAEIGYYSRPIDIFPHSTISLSSKLWIGPEIQNKMAVIASNLDLTVDYGWLWFLSQPLFKLLNFLYNICGNWGVSIILITFIIKGITFPLTKSQFKTMAKIRKLQPKINYIKKKFKNNNQKISEEIMSLYKTEKVNPLGGCFPLFIQMPIFLALYYMLISSVELRHAPFFLWIHDLSDQDPFYVLPILMGVTMFFIQRVTPSNVTDPVQKKIMNYIPILFTVFFLWFPSGLVLYYLISNLVTIIQQKIIIKALNKTLK
Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins.
Q89B34
P39521
FHL1_YEAST
Pre-rRNA-processing protein FHL1
Saccharomyces
MDGEMAIIESSNHVGTSSPTTETQFTIDSSALKDQETKESITNSPTSEVPIETKLPKSSDIVTEEKHPQNTTTDIENEVENPVTDDNGNLKLELPDNLDNADFSKLLEFDAKNDEALFNSNELLSHTMDPVNNIDLTHDHSREVSSKEDINIEPVNPDEDEREKTQDNTAAVKTEGIRNSEDTSIQKDEPTADAIYTDVHKLSVNKDTETLPTLVDEKNNMLHMRNNSITPIMFQQHELVGQPPQNTVTENNSTDAETTQRKLSEPIDASLPLPNEQPTIFAYARLDFQSFTFYVQTLHAIIGRRSENDFSHKVDVNLGPSKSISRRHAQIFYNFGTGRFELSIIGKNGAFVDDIFVEKGNTVPLRNKTKIQIGQIPFQFILPEQERNDDSKSPENADIAESEINTRNLKKNEPKSKKKITTGAKPKKAQTKPAVKKEKKPPKIPKKVYTLEEIPVEYRTKPTVSYSAMLTTCIRKYSTAKGMSLSEIYAGIRELFPYYKYCPDGWQSSVRHNLSLNKSFRKVSKEGKGWLWGLDEEYIAERERQKKKQSEIAVAKAQAAQLKLEQQQHKLQQVPQRGKKDIVSQRSNVNARKQNISQTLAANRAASNRKNTASDNQRTMKYLQEQLVILTRDRKGLSKQVIAAILTQALAMTINQVTQAAKNKGITGNPLTALMDKNPQHLNLILAAAVNAATAKVTKGEVKQLVNPETTAAAALAAKAQHSKPIRQPIVQTPHVPDRPPSQLSASASSHPNNYLHDKQPGSFDPSSLSRFFQPRQNARATSSVAATSVPAAASQNVDAQPKPKPAQDNDLESESGTSSSSSSSSESGSESDSGSDDGSASGSGDNSSTSSESESESDSGSEVDEKNNKNEKIDSESIKNNESKDDIPSKDENSSNDNREISKTDEEGHDSKRRKVSEDINEGITEVNVSLEEKL
Controls the pre-rRNA processing machinery in conjunction with IFH1. Presumably acts as a transcriptional regulator of genes specifically involved in that process. IFH1 convert FHL1 from a repressor to an activator.
P39521
Q0Q028
DFP3_ANTMY
Putative defense protein 3
Antheraea
MMFAYIVAVVSALALTSAYPTGAPSSTCVSMRPGHLADPQPLPAPYTISTPVNTMKAGDSIEVTISGNTPDDFFRGILLQARQGDNIVGKWTVKDDFSKLLDCGEPDNAVTHANSVDKTTVSYIWTAPEDFVGDVVFLVTIVKVYETFWVAIPSAPVTVLSHK
May have antimicrobial activity.
Q0Q028
Q9W445
MCTS1_DROME
Multiple copies in T-cell lymphoma 1 homolog
Sophophora
MFKKFEEKDSISSIQQLKSSVQKGIRAKLLEAYPKLESHIDLILPKKDSYRIAKCHDHIELLLNGAGDQVFFRHRDGPWMPTLRLLHKFPYFVTMQQVDKGAIRFVLSGANVMCPGLTSPGACMTPADKDTVVAIMAEGKEHALAVGLLTLSTQEILAKNKGIGIETYHFLNDGLWKSKPVK
Regulates translation as part of a complex with DENR. Specifically required for translational re-initiation in mRNAs containing upstream open reading frames (uORFs). Not required for standard translational initiation. Regulates expression of a subset of gene products including mbc, InR and EcR.
Q9W445
B8EN93
MINE_METSB
Cell division topological specificity factor
Methylocella
MNFMSFFKRPSTAPVAKDRLKLLLAHERVAIGNSDVVALLREEIVAVIAKHFPVESNAIKVRMETGEAISTLEVEVEIPTPLCVNVRLNANDDAKKKAEHQSRPIEAAAGG
Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell.
B8EN93
Q65KI6
QUEC_BACLD
Queuosine biosynthesis protein QueC
Bacillus
MKQEKAIVVFSGGQDSTTCLLWALRQFQEVEAVTFQYNQRHKQEIEVAKKIAAKLGVKHHLLDMELLNQLAPNALTRDDIEIEAKEGELPSTFVPGRNLVFLSFASILAYQVGARHIITGVCETDFSGYPDCRDEFVKSCNVTVNLAMERPFVIHTPLMWLNKAETWELADELDALDFVKNETLTCYNGIIADGCGECPACKLRANGYNEYMKMKKERA
Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Q65KI6
P31225
CBP1_CANAL
Corticosteroid-binding protein
Candida
MSRTKSTKVLIIGAGVSGLKAAETILSKSFLTGDDVLVVEAQNRIGGRLKTTDTSQSKLGINYDLGASWFHDSLNNIVLNHMINDGLLDDEKDVYFDDKDLKTFSSTGEVPIVDKKLNRVLEDIEKYIQLYFNRNLGVPDLSLRDIVAQYFEKYNRLITEEQREYCGRMMRYLEFWFGISWDRISGKYAVTTHQGRNLLNKKGYGYLVESLAKRIPESSLLLEEPVNKIIRNNKDAGKRVLVETINGLQIFCDYLIVTVPQSILSLEESSPYSIKWEPKLPQRLVESINSIHFGALGKVIFEFDRIFWDNSKDRFQIIADHTDGDLSRELTELPKPFTYPLFAVNFGRVHNGKASLVILTQAPLTNYLETHPDQAWQYYQPMLQKLSINDEPIPDPINTIVTDWTTNPYIRGSYSTMYTNDDPSDLIISLSGDFEDLGISEPYIKFAGEHTTSEGTGCVHGAYMSGIYAADCILENIFRNDVTGYTIIG
May be a flavoprotein with enzymatic activity.
P31225
Q8SJZ1
CYB_PTEVA
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
Pteropus
MTNIRKSHPLFKIINDSLIDLPAPSNISSWWNFGSLLGICLAIQILTGLFLAMHYTSDTTTAFQSVTHICRDVNYGWILRYLHANGASMFFICLFLHVGRGLYYGSYMYKETWNVGVILLFAVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTKLVEWIWGGFSVDKATLTRFFAFHFLLPFIISALVLVHLLFLHETGSNNPTGVPSDSDMIPFHPYYTIKDMLGALVMILALLMLVLFSPDLLGDPDNYIPANPLNTPAHSKPEWYFLFAYAILRSIPNKLGGVLALVLSILILILMPLLHTSKQRSMMFRPLSPCMFWLLVADLLTLAWIGGQPVEHPCIIIGHFASILYFLLILVLMPIMSIVDNHLLKW
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.
Q8SJZ1
Q54K32
RGAA_DICDI
Developmental gene 1029 protein
Dictyostelium
MNKEEYSDISDSESEEVHETNNHNEHEHEEEDDTPEIVVPERKFLKEDEDYSVPFPVMRECLVLLLQSRRILRDMMYYRFKMDRFLSGNLSVFEIQNLLHSQREDKESDWIAEIQELKRNLVSEVRRNHTLERDLNRLDKRIALLIKNRGNIQDVLADKAGLKAPKHKGDQKKPELINDPKKLEAYQNLFYLLQTEPKYLAGLVYLIQPEQMESFLGTVILTLFGDAFTPREEFLLLSLYRLSIQKEMANIATVGDFLKADTVVPKMIITYNKRKQGTDYLKAVIGPILSNVIKQELNLELKPNLVYAAIISEQEIRTGEKSTLDRNVSHEKALEVPEVTKTIKARVDQLISICEQFLDGIISSLNRLPYGIRWICKQIYQIAEKNFTKSTQDEILKVIGYFIYYRFIQVAMVSPEEYDLVGREIHPTARKNLINVSKVLQALFNFAQFGSSEKHFIPLNGWITSHMGDIKNYLQEIIEVGEPEDYLQVDKYMELTQKTKPVIIISLPEICNTHQLISKNLDSLVAKGEKDDPMRIIMKELDEFGPPPDIAADDDREVQLTLSNKFQKTIEEELSPGESLLSQTKEMVISLLRALPTLPEQKDQSDEPPNLVDVLNKARQADPSLEPEIKKILDNLKKLEEYNLTTSADNYSSFLKAVALEVVNRAEIREQQKKEKQRLTTSLNNLRKHQKYLNEQIAQYNQYLQDCRLKHYQNKSKKKKKGDGAKVGPFKFSFSELHKKGVIVDSEVPQITRKKIKFVISSDTVGVFDVSAKMAGIDVQTMRLELDDLLELNSIGTTTLELDQITLDVNMTIHLLNKLFLY
Part of signaling pathway that is required for completion of cytokinesis. gapA and rgaA control cortexillin localization to the cleavage furrow and hence may be involved in cleavage of the midbody in the final stage of cytokinesis by regulating the actin cytoskeleton. Forms a complex by linking activated rac1A to ctxA. Assembly of this complex is necessary for the recruitment of cortexillin to the midzone of a dividing cell. Overexpression leads to the suppression of the formation of cellular projections containing F-actin and to a defect in cytokinesis.
Q54K32
P0DO14
C71A5_GELSE
Cytochrome P450 71AY5
Gelsemium
MEVMQLSFSYPALFLFVFFLFMLVKQLRRPKNLPPGPNKLPIIGNLHQLATELPHHTLKQLADKYGPIMHLQFGEVSAIIVSSAKLAKVFLGNHGLAVADRPKTMVATIMLYNSSGVTFAPYGDYWKHLRQVYAVELLSPKSVRSFSMIMDEEISLMLKRIQSNAAGQPLKVHDEMMTYLFATLCRTSIGSVCKGRDLLIDTAKDISAISAAIRIEELFPSLKILPYITGLHRQLGKLSKRLDGILEDIIAQREKMQESSTGDNDERDILGVLLKLKRSNSNDTKVRIRNDDIKAIVFELILAGTLSTAATVEWCLSELKKNPGAMKKAQDEVRQVMKGETICTNDVQKLEYIRMVIKETFRMHPPAPLLFPRECREPIQVEGYTIPEKSWLIVNYWAVGRDPELWNDPEKFEPERFRNSPVDMSGNHYELIPFGAGRRICPGISFAATNAELLLASLIYHFDWKLPAGVKELDMDELFGAGCVRKNPLHLIPKTVVPCQD
Involved in monoterpene indole alkaloids (MIAs) biosynthesis . Converts by cyclization the strictosidine-derived geissoschizine to the sarpagan alkaloid polyneuridine aldehyde . Converts by aromatization the tetrahydro-beta-carboline alkaloids tetrahydroalstonine and ajmalicine to the corresponding beta-carboline alkaloids alstonine and serpentine, respectively .
P0DO14
P9WEX6
DPMAA_METAN
Diterpenoid pyrone biosynthesis cluster protein A
Metarhizium
MRVNTPSLLICGPMISQADAAYLPQVRSNLVHNKNLSYLREAVSELPNLWLRLVREEPSLGEIDVALFLDNLSQWVKGNSTQPTASRDSRNTQWAVLTVLVQIVEYMEYLDNFSSRDEDGCGHLDAHAALLDHLHEGGIQGLCIGLLTALALACAPSHTEIAKYGAVAVRLALCCGAYIDLNEAKSPAKTICVTTRWPGDDGDDKGDIDRKCDEQLQAILDKYPDAYKSVQTDVSTATITSNEGNVLALLTELEKDGAISKRIDLHGRYHYGGNQAALDKLLQLSSALPMLQFPRRSRLVVPVRNNCNGNIVEDNTALHEMALRCILVENAEWFKTISSSISANTRQAQLLVLGPVNCVPRSLLLRSPQPISLSVSGKADNIYPDQSIAIIGSSCCFPGAENPRQLWEFIRTKQTRGVVDAAGSFDCSFFRKSPREAEYMDPQQRLGLHLAQEALESGGYFSPSSSATKNVGCYLGISSCDYEDNVNSHPPTAYSFTGTARAFASGRISHFFGLTGPSMVIDTACSSSGVAINTACRAIQSGECTMALAGGINLISREARTQENLAAASFLSPTGQCRPFDSKANGYRRGEGGGLVLLKKLSSAVADGDVVLGVIAATAVNQSEGNKSITLPSSESQTSLYRRVLESANMKPRHISYVEAHGTGTQKGDPIECQSIRTVFGGTLRPACRQLHVGSIKSNIGHSEAASGIAALLKVLQMLHHRVIPPQANFEELNPAISPLHDDNIEISRQTKPWEERFRAALVNNYGASGTNAAMLVCQPPSIQHSLPLFPNRPCHYPILLTSHSNESLQLYCRNILRFIENQNNVDSDEEVLANTAFHLAQRQDHSLSFRLTFSVSSIEELKSKLQQQSTSQSYKDGPIQKHSGQPVVVVLAGQTGRRVRLSHEIYASSELLQRHLGRCDRALQTMGFTSLFPGIFDTEPVEDLVQAHCMLFSLQYSVAMSWVDSGLKIDALVGHSLGQLTALCISGMLSLQDGLKLISGRASLIQSKWGAECGAMLSVDADAETVQNLADSLPAGYKVEIACYNSSQSHVVVGTKAAITAFEKAADLRGVSLRRLAISHGFHSEMIDGILPDYNKLVQGLVLHPPAIAIEPCSQSGHSWANATPEIIARQSREPVYFANAISRLEKRFGSCIWLEAGWGSAGVNMARRALTHGPTRSLSTHSFYPAALGEPDSVKALADTTINLWNAGIRVQFWLYHRSQTGSPAPLELPLHPFMKSEYLLPVVKHSKKAQNEKVGQPVIQEKATLVSLIGKTQNAGVQTVEYSINQNSEEYSVYVRGRTVFEHFLAPVSMYIESATRAFRLLSTHKLVSFSTSASMELKNLKLHAPFGFDLQKSLRMILRKLGEDAWEFRVESHPIHEKERGSILQATGVITLQEVYSHLAPHRPVLRRLYDRCEELGKDVSASVVQGDFIKKIINSVARYDDRYIGVRSITSKGFETVAHVFEPEIASQFNPTSPFNPLLLDNFLLIAEIQANNLGGVTPDEIYVGNGFDAATAYTNAEDSEPSTKGHWVGLYSFDHQENDGILCDIFIFCAERKILSMTILGAKFQKIAISSLKRALKTINGVPQTSGGRTPSSSITEFISGDDASPCPPIPGADKPIFIREDDFGSMTTSGHMDEENHLIPEYDVISGSSRSTSSSPPSLESRSQAMETEEITEGAGSALFNLLSNHLNYPKGLSPDTPLGALGLDSLVAIQLQSDIEQMFGKNSQLMDINESSTFSTLFHTIFPQQQTDQFGFVPLHDQTGKDRLESAVPLRLGYSHIKHAAPSFNDSLDRSNTLFIRQVPHAMDALKQNISSTIKAAGFHDFFSDVHPRQRSLVLAYIVQAFRELGCDIRSLRVGDELPSVQFKPKYQNLMNRLFDILGSEGVINVLNKRYLGGLASFPERSAEDMHKAILNDYPSYHPDHKLLHTTGARLADCISGKVDPLQILFQNAASIKLLEDVYVKSPMFGTGNLLLGEFMNCLFSYNKTPDRLNHIRILEIGAGTGATTQLVVDRLLACNVDFTYTFTDVSAALVASAREKLTTRYGQHQRFDMEFETLNIEKEPPASFAQSYDLVISANCIHATRDLRKSCSNIEKLLRKDGGMLCLLELTRPLEWLDCVFGLLDGWWRFDDHRTYALAGEQDWKTILLQSGFDHIDWTDDGSREAQQLRLITAWR
Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the diterpenoid pyrones subglutinols A and B . The first step of the pathway is the synthesis of the alpha-pyrone moiety by the polyketide synthase dpmaA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Probable). The alpha-pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase dpmaD through the action of the prenyltransferase dpmaC to yield a linear alpha-pyrone diterpenoid (Probable). Subsequent steps in the diterpenoid pyrone biosynthetic pathway involve the decalin core formation, which is initiated by the epoxidation of the C10-C11 olefin by the FAD-dependent oxidoreductase dpmaE, and is followed by a cyclization cascade catalyzed by the terpene cyclase dpmaB (Probable). The dehydrogenase dpmaF is then involved in tetrahydrofuran (THF) ring formation at the C5 unit to complete the formation of subglutinols A and B .
P9WEX6
Q255E6
RPOB_CHLFF
Transcriptase subunit beta
Chlamydia
MFKCPERVSVKKKEDILDLPNLIEIQIKSYKQFLQIGKLAEERDNVGLEEVFREIFPIKSYNEATILEYLSYNLGVPKYSPEECIRRGITYSVTLKVRFRLTDETGIKEEEVYMGTIPIMTDKGTFIINGAERVVVSQVHRSPGINFEQEKHSKGNILFSFRIIPYRGSWLEAIFDINDLIYIHIDRKKRRRKILAMTFIRALGYSSDADIIEEFFQIEECSLKSEKDFSVLVGKILADNVLDEASSLVYGKAGEKLSTAMLKRMLDADISTLKIALEADENHPIIKMLAKDPTDSYEAALKDFYRRLRPGEPATLANARSTIMRLFFDPKRYNLGRVGRYKLNRKLGFPMDEESLSQVTLRKEDVIGALKYLIRLKMGDEKASIDDIDHLANRRVRSVGELIQNQCRSGLARMEKIVRERMNLFDFSSDTLIPGKIISAKGLTSVLKDFFGRSQLSQFMDQTNPVAELTHKRRLSALGPGGLNRERAGFEVRDVHASHYGRICPIETPEGPNIGLITSLSSFAKINEFGFIETPYRIVRDGVVTDEIEYMTADVEEECVIAQASANLDEYNMFTDPVCWARYRGEAFEADTSTVTHMDVSPKQLVSIVTGLIPFLEHDDANRALMGSNMQRQAVPLLKTEAPIVGTGLEARAAKDSGAIVVAEEDGVVEYVDGYKVVVAAKHNPTLKRTYEFKKFLRSNSGTCINQRPLCSVGDIVVKGDVIADGPATDQGELALGKNILVAFMPWYGYNFEDAVIISEKLIKQDAYTSIYIEEFELTARDTKLGKEEITRDIPNVSEEVLANLGEDGIIRIGAEVKPGDILVGKITPKSETELAPEERLLRAIFGEKAADVKDASLTVPPGTEGVVMDVKVFSRKDRLSKSDDELVEEAVHLKDLQKGYKNQISVLKTEYREKLGALLLNEKAPASIIHRRTADILVQEGTVFDQETIELLEQESLVDLLMPPCDMYDVLKNLLSDYETSLQRLEVNYKTEVEHIREGDADLDHGVIRQVKVYVASKRKLQVGDKMAGRHGNKGVVSKIVPEADMPYLANGETIQMILNPLGVPSRMNLGQVLETHLGYAAKTAGIHVKTPVFEGFPESRIWDMMIEQGLPADGKSYLYDGKTGERFDNTVVIGYIYMLKLSHLIADKIHARSIGPYSLVTQQPLGGKAQMGGQRFGEMEVWALEAYGVAHMLQEILTVKSDDVSGRTRIYESIVKGENLLKSGTPESFNVLIKEMQGLGLDVRPMVVDA
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Q255E6
A5ELL1
RL18_BRASB
50S ribosomal protein L18
unclassified Bradyrhizobium
MSRAKVTNARRKQRVRLSLRRSAGGRPRLSVFRSSKHIYAQVIDDQKGETLASASSMEKEMRSSGNTGADIDAAKAVGKLLAERAVKAGIKEVVFDRGGYLYHGRVKALADAARESGLSF
This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
A5ELL1
A0LG38
IXTPA_SYNFM
Nucleoside-triphosphate pyrophosphatase
Syntrophobacter
MEHAILVIATRNKGKSREIGKYLEHFPVEVRDLNDFGPIPEVVEDGATFEENAYKKALLTARVLGLPALADDSGLEVAALGGAPGIHSARYAGPDASDAANNEKLLAALSGVEDRAARFCCVLSLAVPSGPALTYEAFCEGTILTAPRGDNGFGYDPLFHYAPAGKTFAEMSLDEKAKVSHRGRALLELQREFDQVLKWLHARTADENLRRGVGHDMCVTGEDPRGTEPKME
Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
A0LG38
A0PTT6
YBEY_MYCUA
Endoribonuclease YbeY
Mycobacterium
MSIEVSNESGIDVSETELVSVARFVIGKMDVNPGAELSMVLLDTAAMADLHMRWMDLPGPTDVMSFPMDELEPGGRPDAPEPGPAMLGDIVLCPEFAAEQAAAAGHSLGHELALLTIHGVLHLLGYDHGEPDEEKEMFALQDRLLEEWVAEQVQAYQQDRQDERDRRLLDKSRYFDEP
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
A0PTT6
B5F503
DNAT_SALA4
Primosomal protein I
Salmonella
MSSRILTSDVIGIDALLHDHHAVLAKSTGGAVAVFANNAPAFYAVTPARMAELLALEEKLSRPGSDVALDAQFYEEPEAAPVAIPCGKFAMYPAWQPDADFQRQAALWGVALREPVTAEELAAFIAYWQAEGKVFHHIQWQQKLARSVQISRSSNGGMPQRDINSVSEPDNHIPPGFRG
This protein is required for primosome-dependent normal DNA replication; it is also involved in inducing stable DNA replication during SOS response. It forms, in concert with DnaB protein and other prepriming proteins DnaC, N, N', N'' a prepriming protein complex on the specific site of the template DNA recognized by protein N'.
B5F503
Q1XD93
CHLI_NEOYE
Mg-protoporphyrin IX chelatase
Neopyropia
MNSTTKENKETIRPVFPFTAIVGQEEMKLALILNVIDPKIGGVMIMGDRGTGKSTTIRAIADLLPKIEVVKDDLFNSHPMDVDLMSDENKKTLQDGVALTTSYINVPMVDLPLGATEDRVCGTIDIEKALTEGIKTFEPGLLAKANRGILYVDEVNLLDDHLVDILLDSAASGWNTVEREGISVRHPARFVLVGSGNPEEGELRPQLLDRFGMHAEIRTVKDPELRVKIVEQRTNFDQNPRRCIEDCQKTQNDLKEKIAEAQLLLSNITIDYDLRIKISQVCGELDVDGLRGDIVTNRAAKAYAAFNGQQNVKSSDIGKVITLCLRHRLRKDPLEAMDSGEKVQKVFNKIFEEEN
Involved in chlorophyll biosynthesis; introduces a magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
Q1XD93
Q12797
ASPH_HUMAN
Peptide-aspartate beta-dioxygenase
Homo
MAQRKNAKSSGNSSSSGSGSGSTSAGSSSPGARRETKHGGHKNGRKGGLSGTSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGIYDADGDGDFDVDDAKVLLGLKERSTSEPAVPPEEAEPHTEPEEQVPVEAEPQNIEDEAKEQIQSLLHEMVHAEHVEGEDLQQEDGPTGEPQQEDDEFLMATDVDDRFETLEPEVSHEETEHSYHVEETVSQDCNQDMEEMMSEQENPDSSEPVVEDERLHHDTDDVTYQVYEEQAVYEPLENEGIEITEVTAPPEDNPVEDSQVIVEEVSIFPVEEQQEVPPETNRKTDDPEQKAKVKKKKPKLLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCEDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLKLSLKRRSDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRFYFHLGDAMQRVGNKEAYKWYELGHKRGHFASVWQRSLYNVNGLKAQPWWTPKETGYTELVKSLERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGDWSQFTLWQQGRRNENACKGAPKTCTLLEKFPETTGCRRGQIKYSIMHPGTHVWPHTGPTNCRLRMHLGLVIPKEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHPELTPQQRRSLPAI
Membrane-bound Ca(2+)-sensing protein, which is a structural component of the ER-plasma membrane junctions. Isoform 8 regulates the activity of Ca(+2) released-activated Ca(+2) (CRAC) channels in T-cells.
Q12797
Q56957
AIL_YERPS
Attachment invasion locus protein
Yersinia
MVFMNKTLLVSSLIACLSIASVNVYAEGESSISIGYAQSRVKEDGYKLDKNPRGFNLKYRYEFNNDWGVIGSFAQTRRGFEESVDGFKLIDGDFKYYSVTAGPVFRINEYVSLYGLLGAGHGKAKVSSIFGQSESRSKTSLAYGAGLQFNPHPNFVIDASYEYSKLDDVKVGTWMLGAGYRF
Promotes the invasion of pathogenic bacteria into eukaryotic cells by an unknown mechanism.
Q56957
P46445
CYC6_SYNY3
Soluble cytochrome f
unclassified Synechocystis
MFKLFNQASRIFFGIALPCLIFLGGIFSLGNTALAADLAHGKAIFAGNCAACHNGGLNAINPSKTLKMADLEANGKNSVAAIVAQITNGNGAMPGFKGRISDSDMEDVAAYVLDQAEKGW
Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis.
P46445
B8D935
FABZ_BUCA5
Beta-hydroxyacyl-ACP dehydratase
Buchnera
MNVINNTLNIKKIFKILPHRYPFLLIDRVLNFEKFKYLQAIKNCSINEPYFQGHFSNEPVFPGVLIIESMAQAASILIYKSTGELNINKLYYFVGVDDTRFKKIAIPGDQIFIKVTILKSNKNILIFKNIAVVNNDIICKSKIVFAKKYLF
Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
B8D935
A5II55
SYM_LEGPC
Methionyl-tRNA synthetase
Legionella
MTSERKMLVTSALPYANGHLHLGHLVEHIQTDIWVRTHKMLGIQCISVCGDDAHGTPIMLKAEQLGITPEALTAEIKLSHEKDFKAFAIDYDYYHTTHSPENQALATTIFERLQAGGDIVKKTIRQFYDPVKQMFLPDRYVKGTCPKCAAVDQYGDNCEVCGATYSPTDLINPVSVISGASPVEMESEHYFFDLPRYEELLKDWTRKGHLQTEVTNKLSEWFEAGLKQWDISRDAPYFGFPIPGVPDKYFYVWLDAPIGYMASFKKYCDERGVSFDEFWDKASKTELYHFVGKDIVYFHALFWPAMLAASGFRTPTAVYTHGFLTVEGQKMSKSRGTFIEARAYLAHLHPEYLRYYFAAKLNGRVDDLDLNFDDFVNRVNADLVGKVVNIASRCAGFINKRFDNRLSSELINQKLYNDLLSAREFVIDAFVSRDYARAIRQIMDCADKVNQYIDANKPWVLAKDESKLNEVHAICTMGINLFRILITYLKPVLPMMAKASEEFLNSEPLHWGSIDKPLLNHRINTFKPLMVRVEKEKIEAMLVQSKESLMTTPIKENTPVEDSNLISIEDFAKVDLRIAKIVNAEPVEGADKLMRLILDLGDAQKQVFAGIKKAYDAEELIGRLTVMVANLEPRTMRFGVSEGMVLAAGDGQGIYLLQPDAGAFPGMKVK
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
A5II55
P0C2N7
DRS1_CHAGB
ATP-dependent RNA helicase DRS1
Chaetomium
MAPSQKRKSLPDDDFIHTISDNDEPDILDEEEETVPAAVAGRPNKKARTAGAGAVKGKKNKKEKKGKKGGKSAAAGGDGEDGDEEEEEEVTGLWGANDADDGAMDSDFEFVAGGGGEDGLSGFDEEGWGFENAKKGVVGAGGAGQEVKSGVDLDEIIRRRREKKKGKGLEKVEEEEVEVEDMGEVDLDLDDEVLAEDGFGMGMEDGEGGVDEEDKGGEDDDEAASDNDSVATPVQHPDDEASEDDDEEDAEEEARRKEFFAAPEETENVGKKGGLSSFQGMSLSRPILRGLTSVGFTKPTPIQAKTIPIALMGKDVVGGAVTGSGKTAAFVVPILERLLYRPKKVPTTRVVVLTPTRELAIQCHSVATKLASHTDIKFCLAVGGLSLKVQEGELRLRPDVVIATPGRFIDHMRNSASFAVETVEILVLDEADRMLEDGFADELNEILTTLPKSRQTMLFSATMTSTVDKLIRVGLNKPARIMVDSQKQTAVTLAQEFVRLRPGREEKRMGYLGPYLQDPVHRTSHYLLQAEEDCSPDPDHLRLAGAFEHRAPWKHEPGSAFRDGKVNYLLATDLASRGLDIKGIDTVINYEAPQSLEIYVHRVGRTARAGRSGVAITLAAEPDRKVVKAAVRAGKAQGAKIISRVIDAADADKWQDQIDEMDDEIDEILQEEKEEKQLAQIEMQVKKGENLIKHEEEIHARPKRTWFETQEDKKKAKELGRAELNGVRDAMKKKGAGRLSNKDKKKLDSKAERSESKSTGWKKGRAERDGKGAVLNLKKVTKPKSKAPAGRKGRR
ATP-binding RNA helicase involved in ribosome assembly.
P0C2N7
B8HCQ9
GPMA_PSECP
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
Pseudarthrobacter
MTYKLILLRHGHSEWNAKNLFTGWVDVDLNDQGRAEAARGGELLVENNILPDVLYTSLLKRAINTANIALDKADRGWIPVKRDWRLNERHYGALQGKDKAQTLAEYGEEQFMEWRRSYDTPPPPLDDNSEFSQAHDPRYADLGDALPRTECLKDVLVRILPYWESDIKADLKAGKTVLVTAHGNSLRALVKHLDGISDEAIAGLNIPTGIPLVYDLDDDFQPVKPGGTYLDPEAAEQAILAVANQGKK
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
B8HCQ9
A8GCL2
RMF_SERP5
Ribosome modulation factor
Serratia
MKRQKRDRLERAHSKGYQAGILGHPKDYCPYKTTVESRSQWLGGWREAMEDRAVTA
During stationary phase, converts 70S ribosomes to an inactive dimeric form (100S ribosomes).
A8GCL2
Q54GH2
BZPR_DICDI
Probable basic-leucine zipper transcription factor R
Dictyostelium
MDNFENPLLAPDQDVLLYLLDGYSQLQQLQKQQFNIHDDNINYNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNIGSPQIMNENIETNSNDPQYLERLQSIQQQQHQCQTQIQQQLQNYQQQYEDQYQQRQQQYQDQYQKPYSSPPLNFNSIPPITNNNNNNNNNNNNNNNNNNSNSNSNSNSNSNSNSNSNSNSNSNNNNINNNICINNNDISIFLLNNQIQLQPLQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQPTQPTQPTKPIQLTQPIQLTQPTLLEELKDISIQQQLLSAIQQTAQSPQQIHPLQQLQPYQLQSYQQIQASQQLQPYQQLIQLQQLQLQQLEEEKRQQQKQLLLQQQQLQEQQEKLQQQLLQQQKQQLKQKVKQQKQQHQKQQPQQQQQSIQIPPELQNYILNNNNNNNNNNTNKTLSPISEMIQNQFLNNQQTILNQNNSTLQLPTPFYSPQQQQQQHTPISSFIPPPSLPSSPPSPPSPPSPPPQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQLQQQQLQQQQLQQQHQLKESYESKESIKKYNQNIASRNYRLKKKDYIKEIENKIATLSLENNRLEKENGSIRTNGSIEMMRMEPESMKMLMDGKLIIENIKHALIIDDEKSLIYLLHQYHRTIDQRYSLLEKEVNKLINPYTQLRLCCIGYVPKSSPLVLNIFQGPESDKWLNLFKIEANITPEQSIKIDSLRFQYGKVSSRLSNELLELDLIIKRFFIKNVLPTPDTPLLNSDYYSEGELIPNTTTESIAPLNNFELLDFASKLESLKNKIILNASLGLDTFATLCSILTPKQEALLLVRVNLFCIDLHHHDILGEVWTNVNQISNSLSNPLTSFSDSMKKINFSFLQLDNNNNNYHYKIN
Probable transcriptional regulator.
Q54GH2
P0DL69
UNTX_CENLI
Orphan peptide CllNtx
Centruroides
KYCYNDDDCKSECMVVKYCQQGTCYCKGN
May act as a toxin.
P0DL69
Q5XIF3
NDUS4_RAT
NADH-ubiquinone oxidoreductase 18 kDa subunit
Rattus
MAAVSMSVSLRQALLRQRAVATAAVSVCRVPSRLLNTSTWKLADGQTRDTQLITVDEKLDVTPLTGVPEEHIKTRKVRIFVPARNNMQSGVNNTKKWKMEFDTRERWENPLMGWASTADPLSNMVLTFSAKEDAVAFAEKHGWSYDVEGRKVPKPKSKSYGANFSWNKRTRVSTK
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Q5XIF3
P21243
PSA1_YEAST
SCL1 suppressor protein
Saccharomyces
MSGAAAASAAGYDRHITIFSPEGRLYQVEYAFKATNQTNINSLAVRGKDCTVVISQKKVPDKLLDPTTVSYIFCISRTIGMVVNGPIPDARNAALRAKAEAAEFRYKYGYDMPCDVLAKRMANLSQIYTQRAYMRPLGVILTFVSVDEELGPSIYKTDPAGYYVGYKATATGPKQQEITTNLENHFKKSKIDHINEESWEKVVEFAITHMIDALGTEFSKNDLEVGVATKDKFFTLSAENIEERLVAIAEQD
The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity.
P21243
Q92AI7
STP1_LISIN
Serine/threonine phosphatase stp
Listeria
MHAEFRTDRGRIRHHNEDNGGVFENKDKQPIVIVADGMGGHRAGDVASEMAVRLLSDAWKETTALLTAEEIETWLQKTIQEVNKEIVLYAESEMDLNGMGTTLVAAIMAQSQVVIANVGDSRGYLLQNDVMRQLTEDHSLVHELLRTGEISKEDAMNHPRKNILLRALGVEGKVEVDTFVVPFQTSDTLLLCSDGLTNMVPEAEMEEILKSKRTLSEKADVFITKANSYGGEDNITVLLVERNLMQKGRDAS
Protein phosphatase that dephosphorylates EF-Tu.
Q92AI7
P54507
TASA_BACSU
Translocation-dependent antimicrobial spore component
Bacillus
MGMKKKLSLGVASAALGLALVGGGTWAAFNDIKSKDATFASGTLDLSAKENSASVNLSNLKPGDKLTKDFQFENNGSLAIKEVLMALNYGDFKANGGSNTSPEDFLSQFEVTLLTVGKEGGNGYPKNIILDDANLKDLYLMSAKNDAAAAEKIKKQIDPKFLNASGKVNVATIDGKTAPEYDGVPKTPTDFDQVQMEIQFKDDKTKDEKGLMVQNKYQGNSIKLQFSFEATQWNGLTIKKDHTDKDGYVKENEKAHSEDKN
TasA is the major protein component of the biofilm extracellular matrix . It forms amyloid fibers that bind cells together in the biofilm . Exhibits an antibacterial activity against a variety of Gram-positive and Gram-negative bacteria . In laboratory strains, is also involved in proper spore coat assembly .
P54507
P56595
APOC1_CANLF
Truncated apolipoprotein C-I
Canis
MRLILSLPVLVVVLSMVLEGPAPAQAAGEISSTFERIPDKLKEFGNTLEDKARAAIESIKKSDIPAKTRNWFSEAFKKVKEHLKTAFS
Inhibitor of lipoprotein binding to the low density lipoprotein (LDL) receptor, LDL receptor-related protein, and very low density lipoprotein (VLDL) receptor. Associates with high density lipoproteins (HDL) and the triacylglycerol-rich lipoproteins in the plasma and makes up about 10% of the protein of the VLDL and 2% of that of HDL. Appears to interfere directly with fatty acid uptake and is also the major plasma inhibitor of cholesteryl ester transfer protein (CETP). Binds free fatty acids and reduces their intracellular esterification. Modulates the interaction of APOE with beta-migrating VLDL and inhibits binding of beta-VLDL to the LDL receptor-related protein.
P56595
A1VIV0
ATPA1_POLNA
F-ATPase subunit alpha 1
Polaromonas
MQLNPAEISELIKSRIEGLAASSDIRNQGTVVSVADGIVRIHGLSDVMQGEMLEFPATADGTPTYGLALNLERDSVGSVILGEYEHIAEGDTVKCTGRILEVPIGPELLGRVVNALGQPIDGKGPINAKLSDVIEKVAPGVIARKSVDQPLQTGLKSIDSMVPIGRGQRELIIGDRQTGKTAVAIDAIINQKGKGVSCVYVAIGQKASSIKNVVRSLEQAGAMDYTIVVAASASESAAMQYVSAYSGCTMGEYFRDRGEDALIVYDDLSKQAVAYRQVSLLLRRPPGREAYPGDVFYLHSRLLERAARVNEKYVEDFTKGAVKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETSLFNAGIRPAINAGISVSRVGGAAQTKLIKNLSGGIRTDLAQYRELAAFAQFASDLDEATRKQLDRGARVTELLKQSQYSPLSVSTMGATLFAVNKGFMDDVDVKKVLAFESGLHAWLKDKHAPLMAKLEANKAMDKDAEAELTTAVTAFKKSFA
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
A1VIV0
Q10712
AMPL1_SOLLC
Prolyl aminopeptidase 1
Solanum subgen. Lycopersicon
MATLRVSSLFASSSSSLHSNPSVFTKYQSSPKWAFSFPVTPLCSKRSKRIVHCIAGDTLGLTRPNESDAPKISIGAKDTAVVQWQGDLLAIGATENDMARDENSKFKNPLLQQLDSELNGLLSAASSEEDFSGKSGQSVNLRFPGGRITLVGLGSSASSPTSYHSLGQAAAAAAKSSQARNIAVALASTDGLSAESKINSASAIATGVVLGSFEDNRFRSESKKSTLESLDILGLGTGPEIERKIKYAEHVCAGVILGRELVNAPANIVTPAVLAEEAKKIASTYSDVISVNILDAEQCKELKMGAYLAVAAAATENPPYFIHLCFKTPTKERKTKLALVGKGLTFDSGGYNLKVGAGSRIELMKNDMGGAAAVLGAAKALGEIRPSRVEVHFIVAACENMISAEGMRPGDIVTASNGKTIEVNNTDAEGRLTLADALIYACNQGVEKIIDLATLTGAIMVALGPSVAGAFTPNDDLAREVVEAAEASGEKLWRMPMEESYWESMKSGSGDMINTGPGNGGAITGALFLKQFVDEKVQWLHLDVAGPVWSDEKKNATGYGVSTLVEWVLRN
Presumably involved in the processing and regular turnover of intracellular proteins.
Q10712