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
|
|---|---|---|---|---|---|---|
P0CC29
|
NU2C1_ANTAG
|
NADH-plastoquinone oxidoreductase subunit 2 A
|
Anthoceros
|
MKLDFGSFLSDGSSILPECILISSLIIILLIDLTSEKKTYWLYFISLTSLIISITVLLFQLKEEPIFSFSGSFQTDGFNGIFRISIAFSSLLCIPLSMEYMKCTKMAITESLIFLLTATIGGMFLCGANDLIIIFITLECLSLSSYLLSGYTKKDVRSNEAAMKYLLMGGASSSILAYGFSWLYGLSGGKIQLQEIFNGLINTQMYNSTSISIVLIFIIAGIAFKLSLVPFHQWTPDVYEGAPTSVIAFFSVTSKIAGLALATRIFNTVFFSSLNEWHLILEIIAILSMILGNFIAITQTSMKRMLAYSSISQIGYFMIGVIAGDSNGYASMITYMLFYIFMNLGTFACITLFGLRTGTDNIRDYAGLYKKDPLLASFLALSLLSLGGIPPLAGFFGKLYLFWCGWKAGLYLSVSVGLFTSVISIYYYLRIVKLIVTKENEETTSYIRKYKTSSNYLVSKSPIEFSIIICVIGSTFSGIVINPVIAIVEKTISLSSFINN
|
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.
|
P0CC29
|
P58747
|
MOBA_NEIMB
|
Molybdopterin-guanine dinucleotide synthase
|
Neisseria
|
MKTFALILAGGQASRMGGEDKGLALLGGKALIDHVIDRVRPQVSHIAISTNRNLEEYARRSPHIFPDARQWQHFGPLSALCTAANDLQLAAADWLLVVPCDMPYLPDDLVARFETVSKRTPLCNAYYVETPITMHYNIMYIRPQILQSAIPYLFSGMKTLRSWLQQQRARPVRFEFDGHFADLNTQIDLQEG
|
Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
|
P58747
|
A2RF72
|
THII_STRPG
|
tRNA 4-thiouridine synthase
|
Streptococcus
|
MDYSEIMVRHGELSTKGKNRMRFINKLKNNIQDVLAPFPAITVRSDRDRTHVSLNGTDYQPVVEALKLVFGVQALSPVYKLEKSVPLLVTAVQDIMTSLYRDGLTFKIATKRSDHAFELDSRELNSLLGGAVFEVLPNIQAQMKHPDVTLKVEIRDEAAYISYEEIKGAGGLPVGTSGKGMLMLSGGIDSPVAGYLALKRGLDIEVVHFASPPYTSPGALAKAQDLTRRLTRFGGNIQFIEVPFTEIQEEIKNKAPEAYLMTLTRRFMMRITDAIREQRKGLVIVNGESLGQVASQTLESMQAINAVTSTPIIRPVVTMDKLEIIEMAQAIDTFDISIQPFEDCCTIFAPDRPKTNPKLGNAEKYEERFDIDGLVQRAVSGIVVTEITPEIVNDEVENLIDALL
|
Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
|
A2RF72
|
Q5E1G4
|
M1PD_ALIF1
|
Mannitol-1-phosphate 5-dehydrogenase
|
Aliivibrio
|
MTQTTAAVICGEKDIQLRTFELPSISADELLVKNISNSVCLSTYKAALLGSKHKRVPENIDEVPVITGHEYAGVIVEVGENLKDQFKAGDSFVLQPAMGLPTGYSAGYSYETFGGNATYSIIPKIAIDLGCVLPYDGSYYADASLAEPMSCIIGAFHASYHTTQFVYEHEMGIKEGGTLALLACAGPMGIGAIDYAINGPVKPRRIVVTDIDEDRLSRAESLIPVSAAKAQGIELIYVNTIEMEDPVTYLKSLNDDQGYDDVMVYAAVAQVLEQADALLGNDGCLNFFAGPTDKEFKVPFNFYNVHYESTHIVGTSGGSTGDMVESLELSAQGDINPSFMITHVGGLQAAPHTILNQLDIPGGKKLIYPHIDLPLTAIDNFASLAEQDPFFSELDAILAKNNYVWNQHAEKALLEFYDVSLSV
|
Seems to be involved in mannitol utilization. Complements an E.coli mtlD deletion mutant.
|
Q5E1G4
|
B9MQM8
|
SYS_CALBD
|
Seryl-tRNA(Ser/Sec) synthetase
|
Caldicellulosiruptor
|
MLDLKYIRANPEKVQEGLSKRNKDVSIAPILELDERRRKLLAEVESLKALQNQKSKEVPKLKKEGKDVTDLMNELKDLSDKIKELDSKVKEVEDEIEKILLTIPNIPHESVPVGKDDTENVEVRRWGEVREPDFEIKPHWEIGVNLGILDFERASKVSGSRFTFYRGLGARLERALINFMLDLHIEKHGYTELFPPFLVARKSMIGTGQLPKFEEDAFKTTDDYFLIPTAEVPVTNYHREEILKEEDLPIKYVAYSACFRAEAGAAGKDTRGLIRQHQFNKVELVKFTKPEDSYDELEKLTADAEDVLKELGLPYRVVLLCSGDLGFSSAKTYDIEVWMPSYGRYVEISSCSNFENYQARRANIRFRRKDGKLDYVHTLNGSGLAVGRTLAAILENFQQKDGTVVVPEVLRKYMGTDVIK
|
Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
|
B9MQM8
|
Q4K6B5
|
UPP_PSEF5
|
UPRTase
|
Pseudomonas
|
MPIREIRHPLIRHKLGLMRRADISTKNFRELAQEVGALLTYEATKDLPLESYEIPGWCGPVQVEKIAGKKITVVPILRAGIGMLEGVLSLIPGAKVSAVGVARNEETLQAHTYLEKLVPEIDERLAMIIDPMLATGSSMVATIDLLKKAGCRDIRAMVLVAAPEGIAAVEQAHPDVTIYTASIDQKLNEHGYIIPGLGDAGDKIFGTKQKDS
|
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
|
Q4K6B5
|
P32795
|
YME1_YEAST
|
Yeast mitochondrial escape protein 1
|
Saccharomyces
|
MNVSKILVSPTVTTNVLRIFAPRLPQIGASLLVQKKWALRSKKFYRFYSEKNSGEMPPKKEADSSGKASNKSTISSIDNSQPPPPSNTNDKTKQANVAVSHAMLATREQEANKDLTSPDAQAAFYKLLLQSNYPQYVVSRFETPGIASSPECMELYMEALQRIGRHSEADAVRQNLLTASSAGAVNPSLASSSSNQSGYHGNFPSMYSPLYGSRKEPLHVVVSESTFTVVSRWVKWLLVFGILTYSFSEGFKYITENTTLLKSSEVADKSVDVAKTNVKFDDVCGCDEARAELEEIVDFLKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEVYVGVGAKRIRDLFAQARSRAPAIIFIDELDAIGGKRNPKDQAYAKQTLNQLLVELDGFSQTSGIIIIGATNFPEALDKALTRPGRFDKVVNVDLPDVRGRADILKHHMKKITLADNVDPTIIARGTPGLSGAELANLVNQAAVYACQKNAVSVDMSHFEWAKDKILMGAERKTMVLTDAARKATAFHEAGHAIMAKYTNGATPLYKATILPRGRALGITFQLPEMDKVDITKRECQARLDVCMGGKIAEELIYGKDNTTSGCGSDLQSATGTARAMVTQYGMSDDVGPVNLSENWESWSNKIRDIADNEVIELLKDSEERARRLLTKKNVELHRLAQGLIEYETLDAHEIEQVCKGEKLDKLKTSTNTVVEGPDSDERKDIGDDKPKIPTMLNA
|
Catalytic subunit of the mitochondrial inner membrane i-AAA protease supercomplex required for mitochondrial inner membrane protein turnover. The protease is probably ATP-dependent. Important to maintain the integrity of the mitochondrial compartment. Required both for the degradation of unassembled subunit 2 of cytochrome c oxidase (COX2) and for efficient assembly of mitochondrial respiratory chain. Binds unfolded substrates in an ATPase-independent manner; binding of folded COX2, a physiological substrate, requires an active ATPase but when COX2 is destabilized an active ATPase is no longer necessary.
|
P32795
|
Q7T3S5
|
B3G5A_DANRE
|
UDP-GlcNAc:beta-Gal beta-1,3-N-acetylglucosaminyltransferase 5A
|
Danio
|
MFMNCRRVKKWHFLQLLSMCCVMSVLMVCWEHVDHHVVSHVKSYSYRYLINSYDFINKSLSVSPEEAARFGSFPYLLDRRDVCKNKDVLLLLFVKSSPGNFKRRQAIRSTWGNESYISQELGVVVKVVFAMGVRPDRSGHKTMQRELRKEHMAHHDLIQQDFLDTFHNLTVKLLLQFRWTHENCAHAHFLMSADDDVFIHVPNLVHYLQELKSQNVRNLWVGHVHRGAPPVRKRDSKYYMPFDMYQWSSYPDYTAGAGYVVSGDVAAKIYQATQSLNASMYIDDVFMGICAIAAGVSPQEHVYFSGEGKTPYHPCIYEKMITSHGHEGDIRYLWKAATGPQVEGISSGLLGKLYCAAVKMTLLCKPYFTNTYSCMAAFT
|
Beta-1,3-N-acetylglucosaminyltransferase that plays a key role in the synthesis of lacto- or neolacto-series carbohydrate chains on glycolipids.
|
Q7T3S5
|
O83041
|
PIP_LEPBY
|
Prolyl aminopeptidase
|
Leptolyngbya
|
MRQLYPAIAPYQSGMLPVSALHTIYYEQSGNPNGKPVVFLHGGPGGGTIPTYRQYFDPSKWRIILFDQRGAGKSTPHAELRENTTWDLVSDIEKLRSHLNIDRWFVFGGSWGSTLSLAYSQTHPDRCLGLILRGIFLLRRKEILWFYQDGASWIFPDAWEHYLEPIPPEERDDMISAYYRRLTSKDAEIRSTAAKAWSVWEGTTSRLIVDPSLQSKFADDEFADAFARIECHYFINRGFFETDDQLLQNCDRIAHIPTVIVQGRYDVVCPMTSAWALHKALPESELIVVPDAGHSMMEAGILSALIDATDRFVAQKTNGKI
|
Specifically catalyzes the removal of N-terminal proline residues from peptides.
|
O83041
|
O13919
|
PST2_SCHPO
|
SIN3 homolog 2
|
Schizosaccharomyces
|
MEQTLAILKNDNSTLVAEMQNQLVHDFSPNGTALPELDIKAFVQKLGQRLCHRPYVYSAFMDVVKALHNEIVDFPGFIERISVILRDYPDLLEYLNIFLPSSYKYLLSNSGANFTLQFTTPSGPVSTPSTYVATYNDLPCTYHRAIGFVSRVRRALLSNPEQFFKLQDSLRKFKNSECSLSELQTIVTSLLAEHPSLAHEFHNFLPSSIFFGSKPPLGSFPLRGIQSSQFTLSNISDLLSQSRPDNLSPFSHLSNESSDFFKNVKNVLTDVETYHEFLKLLNLYVQGIIDRNILVSRGFGFLKSNSGLWRSFLSLTSLSPEEFLSVYNSACSDFPECGPSYRLLPVEERNISCSGRDDFAWGILNDDWVSHPTWASEESGFIVQRKTPYEEAMTKLEEERYEFDRHIEATSWTIKSLKKIQNRINELPEEERETYTLEEGLGLPSKSIYKKTIKLVYTSEHAEEMFKALERMPCLTLPLVISRLEEKNEEWKSVKRSLQPGWRSIEFKNYDKSLDSQCVYFKARDKKNVSSKFLLAEADILRSQAKLHFPLRSRSAFEFSFVYDNEIVLFDTCYMVCTYIVCNSPSGLKKVEHFFKNILPLHFGLEKDKFSIFLDQVFRGPDYDVNAPNIVGNKPVRRKRSNSITQLTEFVKQPKINGQRESRSAAAARKKEESGNKSQSNSQNSLSDESGNVTPVSKKQLSQPAAAIKASLKYPSHPDSLLEHQDHAGDTENEMHDDVDKEQFGYSSMYVFFRLFNLLYERLYELQRLEDQVSIIQQRIIPNPVSQKQKIWRDRWNDLSDVPDEKTHYENTYVMILRLIYGIVDQSAFEDYLRFYYGNKAYKIYTIDKLVWSAAKQVHHIVSDGKYKFVTSLVEQNSSASPKKNYDDFLYRLEIEKLLNPDEILFRFCWINKFKSFGIKIMKRANLIVDQSLDTQRRVWKKYVQNYRIQKLTEEISYKNYRCPFLCRNIEKERTVEQLVSRLQTKLLRSAELVSGLQAKLCLDSFKLLYLPRTEDSYIDASYLRLRDTDFLDCQNKRKQRWRNRWESLLKSVRGTSDNTAEVNFDADINALFIP
|
Has a role in chromatin assembly and chromosome segregation. Involved in the deacetylation of histones.
|
O13919
|
Q8PPA8
|
MURG_XANAC
|
Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase
|
Xanthomonas
|
MSVSANAAQAHAQPSAVLRPVMILAGGTGGHIFPGLAVAKVLRARGVPVTWLGADGAMETRLVPQHDIPIDTLAISGLRGKGVVKLLGAPVRVMRAVRAAGFVLRKRQPRAVISFGGFAAGPGGLAARLLGAPLLVHEQNRAPGMTNKVLSRFARRVLTGFPGSFVGEEAVGNPVRAEIAALPAPADRLFGRTGPVRVLVLGGSQGARVLNQALPAALVALGHSEVEVRHQCGEKLRAEAEAAYAQAGVNASVEPFIADMAAAYAWADLVVCRAGASTLAELCAAGVGSVLVPFAAAVDDHQTRNAEYLVGANAAVLLKQDDSLPVRLQQVLQTLLADPARRLSMANAARTLAKPDAAERIADIILQEAGNGPSGMGNGHSSEQPQERTLMHADKRTDQVSVAAGAQLHTIPDSRFPIRTSTGGAR
|
Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
|
Q8PPA8
|
D7BSS4
|
MSHC_STRBB
|
Mycothiol ligase
|
Streptomyces
|
MYAWPASEVPALPGRGRDLRIHDTATGGPLTLDPGPVARIYVCGITPYDATHMGHAATYNAFDLVQRVWLDTKRQVHYVQNVTDIDDPLLERAVANGDDWTALAERETTLFREDMTALRMLPPRHYIGAVEAIPGIVPLVERLRDAGAAYELEGDIYFSVESDPSFGGVSGLDAEAMRLLSAERGGDPDRPGKKNPLDPMLWLAARPGEPSWDGGSLGRGRPGWHIECVAIALDHLGMGFDVQGGGSDLAFPHHEMGASHAQVLTGERPFAKAYVHAGMVALDGEKMSKSKGNLVFVSALRRDGVDPAAIRLALLAHHYREDWEWTDGVLQEAQERLARWRAAVSRPDGPPADALLDEIRTALANDLDAPSALAAVDRWASAQASEGGTDEGAPGLVSRAVDALLGVAL
|
Catalyzes the ATP-dependent condensation of GlcN-Ins and L-cysteine to form L-Cys-GlcN-Ins.
|
D7BSS4
|
A8GYY7
|
RL24_SHEPA
|
50S ribosomal protein L24
|
Shewanella
|
MAAKIRRQDEVIVLAGKDQGKRGKVSQVLPTGKLIVEGINLVKKHQKPNPQLGVAGGIVEQEAPIQASNVAIFNSATGKADRVGFRFEDGKKVRFFKSNSELVK
|
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
|
A8GYY7
|
Q75DX7
|
HEM1_ASHGO
|
Delta-aminolevulinate synthase
|
Eremothecium
|
MDSLARQSAKICPFVSRVTSSMQQVQVLHKTNMSAMAQQCPVMRRAMAARGYVTASPPAGAAAADVGEARPITPVLERGTQERTFDYDGLFETELQKKRLDSSYRFFNNINRLAKEYPMAHRLEEEDKVTVWCSNDYLTYSRNEKVMETMKRTIDKYGAGAGGTRNIAGHNRHAMRLEAELAALHKKEGALVFSSCFVANDAVLSLLGQKMPNMVIFSDEMNHASMIMGIKHANVQKHIFRHNDLQHLEELLAMYPKSQPKLIAFESVYSMSGSVADIRKICDLAEKYGALTFLDEVHSVGLYGPHGAGVAEHLDFEAHRKAGLASPAQTTVLDRVDMITATLGKSFGSVGGYLAASEKLVDFVRSYAPGFIFTSSLPPAVMAGSAAAVFDQRSSLHLRQLQQKHTSYVKTGLGDLGIPVQPNPSHIVPVLVGNPDLAKRASDILMEKHRIYVQAINFPTVPRGTERLRITPTPGHTNDLSDVLLDAMDDVWKTLQLPRVSDWAAHGGLLGVGEPDYVPEANLWTEEQMSLTNDDLHPSVFSPVEKFLEVSSGIKA
|
Catalyzes the synthesis of 5-aminolevulinate (ALA) from succinyl-CoA and glycine, the first and rate-limiting step in heme biosynthesis.
|
Q75DX7
|
Q06J41
|
PSBA_BIGNA
|
Photosystem II Q(B) protein
|
Bigelowiella
|
MTAIIERRENSSLWARFCEWITSTENRLYIGWFGVLMVPTLLTATTVFIIGFIAAPPVDIDGIREPVSGSLLYGNNIISGAIVPTSNAIGLHFYPIWEAASVDEWLYNGGPYQMIVCHFFIGVCSYMGREWELSFRLGMRPWIAVAYSAPVAAATAVFIIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLIRQTTENESTNNGYVFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVIGIWFTAMGISTMAFNLNGFNFNQSIIDSQGRVINSWADIINRANLGMEVMHERNAHNFPLDLA
|
Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors.
|
Q06J41
|
A9MB09
|
KTHY_BRUC2
|
dTMP kinase
|
Brucella
|
MSGLFITFEGGEGAGKSTQIALLASHLRNHGFDPVITREPGGSPGAEAIRHVILSGNAETYGPAMEALLFAAARADHVDQLIRPALAEGRIVLCDRFIDSGRAYQGVTGNLDATYMAAIERIAIDGAMPDLTLVLDICAERGLSRAGKRRGSDTADRFEKEDIAVHEARRQAFLEIARQEPARCKVIDADRSQEKIADEIRSVVDTILTEKGLL
|
Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
|
A9MB09
|
C6E7R9
|
DCUP_GEOSM
|
Uroporphyrinogen decarboxylase
|
unclassified Geobacter
|
MNTRFLDACWGKPVDTVPVWLMRQAGRYLPDYMRVRSKCTFLELCKTPELATEVTVQPVDILGVDAAILFSDILTPIEPMGMELDFTPGPVFAKPIRTMADVEALKIPKMETDVPYVLDAVKLLRKELAAKVPLIGFGGAPFTLACYMVEGKGSKDFAALKKMMYADPEVYAALMEKITTMDMEYLNAQIKAGAQAIQIFDTWGGMLSPADYERYVLPYTQRLINGLDRTNIPVIHFVKGAGTMLEIVKQAGGDVMGLDWHVNLGKARDILGDMAVQGNLDPTVLFAPNEIIEREVKRVLDENAGRPGLIFNLGHGILPTVPPEKAIFMVDCVHRLSRK
|
Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
|
C6E7R9
|
Q6GHG1
|
PNP_STAAR
|
Polynucleotide phosphorylase
|
Staphylococcus
|
MSQEKKVFKTEWAGRSLTIETGQLAKQANGAVLVRYGDTVVLSTATASKEPRDGDFFPLTVNYEEKMYAAGKIPGGFKKREGRPGDDATLTARLIDRPIRPLFPKGYKHDVQIMNMVLSADPDCSPQMAAMIGSSMALSVSDIPFQGPIAGVNVGYIDGKYIINPTVEEKEVSRLDLEVAGHKDAVNMVEAGASEITEQEMLEAIFFGHEEIQRLVDFQQQIVDHIQPVKQEFIPTERDEALVERVKSLTEEKGLKETVLTFDKQQRDENLDNLKEEIVNEFIDEEDPENELLIKEVYAILNELVKEEVRRLIADEKIRPDGRKPDEIRPLDSEVGILPRTHGSGLFTRGQTQALSVLTLGALGDYQLIDGLGPEEEKRFMHHYNFPNFSVGETGPVRAPGRREIGHGALGERALKYIIPDTADFPYTIRIVSEVLESNGSSSQASICGSTLALMDAGVPIKAPVAGIAMGLVTREDSYTILTDIQGMEDALGDMDFKVAGTKEGITAIQMDIKIDGLTREIIEEALEQARRGRLEIMNHMLQTIDQPRTELSAYAPKVVTMTIKPDKIRDVIGPGGKKINEIIDETGVKLDIEQDGTIFIGAVDQAMINRAREIIEEITREAEVGQTYQATVKRIEKYGAFVGLFPGKDALLHISQISKNRIEKVEDVLKIGDTIEVKITEIDKQGRVNASHRALEE
|
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
|
Q6GHG1
|
P31641
|
SC6A6_HUMAN
|
Solute carrier family 6 member 6
|
Homo
|
MATKEKLQCLKDFHKDILKPSPGKSPGTRPEDEAEGKPPQREKWSSKIDFVLSVAGGFVGLGNVWRFPYLCYKNGGGAFLIPYFIFLFGSGLPVFFLEIIIGQYTSEGGITCWEKICPLFSGIGYASVVIVSLLNVYYIVILAWATYYLFQSFQKELPWAHCNHSWNTPHCMEDTMRKNKSVWITISSTNFTSPVIEFWERNVLSLSPGIDHPGSLKWDLALCLLLVWLVCFFCIWKGVRSTGKVVYFTATFPFAMLLVLLVRGLTLPGAGAGIKFYLYPDITRLEDPQVWIDAGTQIFFSYAICLGAMTSLGSYNKYKYNSYRDCMLLGCLNSGTSFVSGFAIFSILGFMAQEQGVDIADVAESGPGLAFIAYPKAVTMMPLPTFWSILFFIMLLLLGLDSQFVEVEGQITSLVDLYPSFLRKGYRREIFIAFVCSISYLLGLTMVTEGGMYVFQLFDYYAASGVCLLWVAFFECFVIAWIYGGDNLYDGIEDMIGYRPGPWMKYSWAVITPVLCVGCFIFSLVKYVPLTYNKTYVYPNWAIGLGWSLALSSMLCVPLVIVIRLCQTEGPFLVRVKYLLTPREPNRWAVEREGATPYNSRTVMNGALVKPTHIIVETMM
|
Sodium-dependent taurine and beta-alanine transporter. Chloride ions are necessary for optimal uptake.
|
P31641
|
A6LGE9
|
YIDD_PARD8
|
Putative membrane protein insertion efficiency factor
|
Parabacteroides
|
MRRFFTTLLLLPVYFYKYCISLMTPASCRYTPTCSEYAVQALKKYGPVKGLYLAVKRILRCHPWGGSGYDPVP
|
Could be involved in insertion of integral membrane proteins into the membrane.
|
A6LGE9
|
E3QKL1
|
MEP_COLGM
|
Fungalysin mep
|
Colletotrichum graminicola species complex
|
MYRSMKSLALLGLLGPTSQVFAHPATGHAHNIGRRGVDIEAFRLPQVGSYTNATEIETTPPIALLKRESYVETATELVKKLAPNSEFRLVGDHYVGTNGIGHVNFKQTVHGLDIDNGDFNVNIGKDGKVFSYGNNFFKGEAPEASPLKKRDFKDPVSALKGAKDVLQLPVEAASASAEPKEGTEVYSIKGTSGTVSDPEARLVYFVKADGSLALSWRVETDITENWLLTYVDAETGTDVHGVVDYVSDLANYRVYPWGVNDPTEGDRVLVTDPWDISASPLTWQSDGTTNYTTTRGNNGIAQSNPSGGTAYLNNYRPTSAARNFDYQYTTSLTTPSSYIDASIAQLYYTANHYHDLLYTLGFTESAGNFQINNNGKGGVGNDFVVLFAQDGSGTNNANFLTPPDGSNGRMRMYLWTMSTPRRDCSFEAGVVIHEYTHGLSTRLTGGPANSNCLNALESGGMGEGWGDFFATAIRLKPTDTRATDYSMGAWVYNNPAGIRSVLYSTSMTTTPNTYSTINGVSSVHRIGETWATTLYEVLWNLIDKHGKNDGPRPEFDSNGVPTDGKYLTLKLVLDGMALQPCSPNFIQARDAILDADKALTGGDNLCELWTAFAKRGLGSNAVYSSSNRRDGFNVPAGVC
|
Secreted metalloproteinase that allows assimilation of proteinaceous substrates.
|
E3QKL1
|
P85040
|
VKTC9_DABSI
|
Chymotrypsin inhibitor C9
|
Daboia
|
HDRPKFCYLPADPGECMA
|
Serine protease inhibitor that inhibits chymotrypsin.
|
P85040
|
Q5PGP3
|
GSIA_SALPA
|
Glutathione import ATP-binding protein GsiA
|
Salmonella
|
MPHSDELDSRDVLSVSGLNIAFHHEGQQIDAVRNVSLRLKRGETLAIVGESGSGKSVTALALMRLIEQSGANVRCGEMLLRRRNRQVIELSEQSDAQMRRVRGADIAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASHEEALAEAKRMLDQVRIPESQAILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQQEMSMGVIFITHDMGVVADIADRVLVMYQGEAVETGSVEQIFHAPTHPYTQTLLAAVPQLGAMRGHSLPRRFPLISADEPALYESQIEQDTVVEGEPILQVRGLVTRFPLRSGLFNRVTREVHAVENISFDLWPGETLSLVGESGSGKSTTGRALLRLVESRQGEIIFNGQRIDSLSAGKLQPLRRDIQCIFQDPYASLDPRQTVGYSIMEPLRIHGLGQGDAAAKRVAWLLERVGLRPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSVRGQIINLLLDLQREMGIAYLFISHDMAVVERISHRVAVMYLGQIVEMGPRRAVFENPQHPYTRKLMAAVPVADPSRHRPRRVLLSDDIPSNIHKRGEETPAVSLQLVGPGHYVARPLQDNALSRL
|
Part of the ABC transporter complex GsiABCD involved in glutathione import. Responsible for energy coupling to the transport system.
|
Q5PGP3
|
A7HD76
|
PYRD_ANADF
|
Dihydroorotate oxidase
|
unclassified Anaeromyxobacter
|
MIWPALRWTLFHLDPERAHRLAHGALHRVPPGLARLRRPAVPPELRVSCLGLDFDGPIGLAAGFDKGDASIAGLFALGFSHVEIGTITPRPQAGNEPPRLFRLVEHRALVNRMGFNNAGAEVCARRLAGVPATARMGPVGVNVGKNKTTPNEDAAADYLACIDRLHPYADYLVVNISSPNTPGLRQLQERDQLDALLRACAGRLRERAPGKPLLVKLAPDLSPTALDEAVDVAIDAGVSGIVATNTTLSRAGVERHPRAREAGGLSGAPLEALATSVVRRCYIRAAGRVPIVGCGGVMNAEGAYAKIRAGATLVQVYTGLVYGGPGFVRRLNDGLARLLARDGFRTVAEAVGADVETAERAGV
|
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
|
A7HD76
|
Q601L2
|
RL2_MESH2
|
50S ribosomal protein L2
|
Mesomycoplasma
|
MALKYYKPTTNGRRHMSSLDFGANLTTNKPEKSLLTILKKHSGRNSQGKITVRHQGGRHKRKYRLIDFKRNKDDIPGIVKTIEYDPNRSANIALISYIDGEKRYILAPKNLKVGQKISSGPKSDILVGNALPLAKIPEGTFVHNIELKPGAGAKLIRSAGTWAQIQGRDEDGKYVILKLKSGEYRRILATCRATIGVVGNEENSLVNIGKAGRNRHKGIRPTVRGSVMNPNDHPHGGGEGKQPIGRKSPLTPWGKKALGVKTRNPKKPSTKLIIRSRKETKK
|
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome.
|
Q601L2
|
P20275
|
PFKA_SPICI
|
Phosphohexokinase
|
Spiroplasma
|
MLKKIGILTSGGDSQGMNAAIAGVIKTAHAKGLETYIIRDGYLGLINNWIEVVDNNFADSIMLLGGTVIGSARLPEFKDPEVQKKAVDILKKQEIAALVVIGGDGSYQGAQRLTELGINCIALPGTIDNDITSSDYTIGFDTAINIVVEAIDRLRDTMQSHNRCSIVEVMGHACGDIALYAGIAGGADIISINEAALSETEIADRVAMLHQAQKRSVIVVVSEMIYPDVHKLAKLVESKSGYITRATVLGHTQRGGNPTAMDRYRAFQMAQFAVEQIIAGVGGLAIGNQGDQIIARPIMEALSIPRSSRKEIWAKFDQLNQNIYQKS
|
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
|
P20275
|
P44812
|
ZAPB_HAEIN
|
Cell division protein ZapB
|
Haemophilus
|
MSLEILDQLEEKIKQAVETIQLLQLEVEELKEKNAESQRNIENLQTENEQLKNEHRNWQEHIRSLLGKFDNV
|
Non-essential, abundant cell division factor that is required for proper Z-ring formation. It is recruited early to the divisome by direct interaction with FtsZ, stimulating Z-ring assembly and thereby promoting cell division earlier in the cell cycle. Its recruitment to the Z-ring requires functional FtsA or ZipA.
|
P44812
|
Q6YR12
|
RS17_ONYPE
|
30S ribosomal protein S17
|
Candidatus Phytoplasma asteris
|
MQRNFRKTFVGKVVSDKMDKTITVIVDIYKKDPLYGKRVKQSKKFHVHDENQEAKPGDLVNFMETRPLSKTKRFRLFKILSHAKSAK
|
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
|
Q6YR12
|
A3CVZ3
|
SPSS_METMJ
|
Sep-tRNA:Cys-tRNA synthase
|
Methanoculleus
|
MKCAVDIESRDVEEMYINIDPIQAGGRLTVDAMKAAISFADGYSVCDNCRSPFRLDYIQKPPIAQFHADLAAWLNMDTARVVPGARRGFQAVASTYVEKGDPVIVTSLAHYTEFVAVEEAGGIPLEVPKDEKNHITPDAAAEKIEAVILEFSKTPPLLFIDHVDYQFGNVHDVAAITKVAHQYDIPVLVNGAYSVGIMPVDGKALGADFVVGSGHKSMAAPAPSGVLATTNEHAERVFRTTQAKGDVTGRTFGIKEVEMMGCTLMGVTVVGMMASFPHVKERVKHWDTEVAHSQAVVDALLSIEGTKVLSDYPRQHTLTRIDTRESFDKVAQQHKKRGFFLSSDLKKRGITGVIPGSTRVWKFNTFGLTEKQIRHVGESFVEIARENGLNIV
|
Converts O-phospho-L-seryl-tRNA(Cys) (Sep-tRNA(Cys)) to L-cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)).
|
A3CVZ3
|
Q88HA3
|
MOBA_PSEPK
|
Molybdopterin-guanine dinucleotide synthase
|
Pseudomonas
|
MPDALPPCSILILAGGRGQRMGGRDKGLVDWQGEPLIAHVHRAVRPLSDDLVISCNRNQAAYQAYADRLVGDAEADFPGPLAGVIAGLRVARHAWVVVLACDAPLVDRELIEGLLRLAVAGNSAAMVRQGGFWQPMFSVLPKRVLPVLEQAWAAGERSLQKALLREAVQGLECAESDRRLSNFNSPERLQD
|
Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
|
Q88HA3
|
B7K508
|
THIC_RIPO1
|
Thiamine biosynthesis protein ThiC
|
Rippkaea orientalis
|
MRSQWVAKRRGQSNVSQMHYARQGMITEEMDYVAKRENLPPDLIRQEVARGRMIIPANINHLNLEPMAIGIASKCKVNANIGASPNSSNLEEEVAKLNLAVKYGADTVMDLSTGGGDLDTIRTAIINASPVPIGTVPIYQAVESVHGNIEKLTPDDFLHIIEKHAQQGVDYMTIHAGLLIEYLPLVRSRLTGIVSRGGGIIAKWMLHHHKQNPLYTHFDEIIEIFKKYDVSFSLGDSLRPGCTHDASDEAQLSELKTLGQLTRRAWEHDVQVMVEGPGHVPMDQIEFNVKKQMEECSEAPFYVLGPLVTDIAPGYDHITSAIGAAMAGWYGTAMLCYVTPKEHLGLPDAEDVRNGLIAYKIAAHAADIARQRPGARDRDDELSKARYNFDWNRQFELSLDPDRAREYHDETLPADIYKTAEFCSMCGPKFCPMQTKVDADALTELEKFLAEQKNKEAIAH
|
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.
|
B7K508
|
A1TQY3
|
PDXH_ACIAC
|
Pyridoxal 5'-phosphate synthase
|
Acidovorax
|
MHNRGMSSPSSPLSSSIADLRKSYERAELGEEASHADPLRQFDQWLQEAVAAQVPEPNAMTLATVGADLRPSTRVVLIKGYDERGIVWYTNYGSRKGRQLAGNPFAALQFHWVELERVVRIEGRVEKVSDAESDAYFASRPLDSRIGAWASPQSEVISGRGVLVANAAKYGAQFLLQPLRPPHWGGFRLKPDRWEFWQGRKSRLHDRLCYREETPGAWVRERLAP
|
Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
|
A1TQY3
|
B3EQL4
|
COAD_CHLPB
|
Pantetheine-phosphate adenylyltransferase
|
Chlorobium
|
MERLAIYPGTFDPFTNGHLDVLERALTIFDKVYIVLAENSKKSSLFTVDERCSMIREITASTSGVSVEVLHGGLLAEYAHSVGATAIVRGLRQVKDFEYEFQLSLLNRHLNPEVTTVFLMPNVKYTYVASSIIREVALLGGDVSKFVHPCVLAMLKKKYEEQNAQ
|
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
|
B3EQL4
|
Q4JVQ1
|
TATA_CORJK
|
Sec-independent protein translocase protein TatA
|
Corynebacterium
|
MPNLGVPELLIIALVIFLLFGATRLPNAARSLGRSMRIFKSEMDEMKTDGDKKELAEKQAPTAEQQQAQDLAQPKSEQPNEHNA
|
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
|
Q4JVQ1
|
A5UFI3
|
FDHE_HAEIG
|
Protein FdhE homolog
|
Haemophilus
|
MSIKILSESEIKQVANSYQAPAVLFANPKNLYQRRAKRLRDLAQNHPLSDYLLFAADIVESQLSTLEKNPLPPQQLEQLNAIEPLNTKTFKRDSIWREYLTEILDEIKPKANEQIAATIEFLEKASFAELEEMANKLLTQEFNLVSSDKAVFIWAALSLYWLQAAQQIPHNSQVENTENLHHCPVCGSLPVASIVQIGTSQGLRYLHCNLCESEWNLVRAQCTNCNSHDKLEIWSLNEELALVRAETCGSCESYLKMMFQEKDPYVEPVADDLASIFLDIEMEEKGFARSGLNPFIFPAEEA
|
Necessary for formate dehydrogenase activity.
|
A5UFI3
|
B8HMQ7
|
RL2_CYAP4
|
50S ribosomal protein L2
|
unclassified Cyanothece
|
MGIRNYRPYTPGTRQKSVSDFSEITHDQPEKSLTSFRHRAKGRNNRGVITSRRRGGGHKRLYREIDFRRNKLSVPGTVLTVEYDPNRNARISLVQYEDGEKRYILHPRNLAVGAVIAAGPDAAIEVGNALPLSKIPLGTGVHNVEITPGRGGQMVRAAGAMAQVVAKEGDMVTLKLPSGEVRLFRKECYATIGQIGNVDVNNISIGKAGRNRWKGRRPKVRGSVMNPVDHPHGGGEGRAPIGRSGPVTPWGKPTLGYKTRKKKKLSNALIVRRRRKSSKRGRGGRQS
|
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome.
|
B8HMQ7
|
A5VKT4
|
SYE_LIMRD
|
Glutamyl-tRNA synthetase
|
Limosilactobacillus
|
MDQKVRVRYAPSPTGFLHIGNAQSALFNYLFARHFDGTMVLRIEDTDTKRNVEDGEASQRENLHWLGIDWDEGPNKPNPKYAPYRQSERNKEGIYHKYIQELLDKGIAYKDYSTEEELAEMRERQKANNEPPHYDGRWYGKSEEEQKAAEAKGLKPTIRFHFPKDHDYEWDDIARGHVSFNSDNLGGDFIIEKSDGMPTYNFAVVVDDHTMDITHVLRGADHISNTPKQIAIYEALGWEHPTFCHIPLIFNPKTRKKLSKRDKDTLQFISEYKKHGYLHEAIFNFIAFLGWSPVGEREIYSKEELIKVYDPKRMSKAPAYFDQKKLDWMNAQYIKSMSIDELTDRTMELIKEGETEEAKRLQSIPEEQLTELLKKTIKVHQRDVNKLLEVIQYAWSYYTVLDQSFNYDLLKDNEDFANEDVLAVLKGLKAKLENGDDDLDYSQAIKEVGKDTGIKGRGLYFPLNLAFTGSTSAPQIYEIMDIYSRDTDIELLDRMIKAFEN
|
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
|
A5VKT4
|
A2C717
|
PRMA_PROM3
|
Ribosomal protein L11 methyltransferase
|
Prochlorococcus
|
MNSASACCWWRLALPIADELEESLIWKLTELGISRIAVQHVPEKAERTLLAWLPSSEWSESDRDQLMVNLRPLAEPFGLQLANPTWCEVADEDWSLNWKQHWQSDPVGQRLLILPAWLDLPQEYADRLVVRMDPGSAFGTGSHPSTRLCLEALEKNPPLGLRVADLGCGSGVLGFAALGFGARQVLAADTDSQAVCASRANAELNQLDLDRFRVVHGSVDALSAQLQGEVVDLLLCNILAPVIEALASSFDQLLSANGRCLLSGLLVDQAPRLQVVLEALGWRVNSLTVQGCWGLLDVSKR
|
Methylates ribosomal protein L11.
|
A2C717
|
Q12469
|
SKM1_YEAST
|
Protein kinase 75490 D
|
Saccharomyces
|
MKGVKKEGWISYKVDGLFSFLWQKRYLVLNDSYLAFYKSDKCNEEPVLSVPLTSITNVSRIQLKQNCFEILRATDQKENISPINSYFYESNSKRSIFISTRTERDLHGWLDAIFAKCPLLSGVSSPTNFTHKVHVGFDPKVGNFVGVPDSWAKLLQTSEITYDDWNRNSKAVIKALQFYEDYNGLDTMQFNDHLNTSLDLKPLKSPTRYIINKRTNSIKRSVSRTLRKGKTDSILPVYQSELKPFPRPSDDDYKFTNIEDNKVREEGRVHVSKESTADSQTKQLGKKEQKVIQSHLRRHDNNSTFRPHRLAPSAPATKNHDSKTKWHKEDLLELKNNDDSNEIIMKMKTVAIDVNPRPYFQLVEKAGQGASGAVYLSKRIKLPQENDPRFLKSHCHRVVGERVAIKQIRLSEQPKKQLIMNELLVMNDSRQENIVNFLEAYIIDDEELWVIMEYMEGGCLTDILDAVARSNTGEHSSPLNENQMAYIVKETCQGLKFLHNKKIIHRDIKSDNILLNSQGLVKITDFGFCVELTEKRSKRATMVGTPYWMAPEIVNQKGYDEKVDVWSLGIMLIEMIEGEPPYLNEDPLKALYLIANNGSPKLRHPESVSKQTKQFLDACLQVNVESRASVRKLLTFEFLSMACSPEQLKVSLKWH
|
May be involved in cellular signaling or cytoskeletal functions. May play a role in morphogenetic control.
|
Q12469
|
Q9P2X0
|
DPM3_HUMAN
|
Prostin-1
|
Homo
|
MTKLAQWLWGLAILGSTWVALTTGALGLELPLSCQEVLWPLPAYLLVSAGCYALGTVGYRVATFHDCEDAARELQSQIQEARADLARRGLRF
|
Stabilizer subunit of the dolichol-phosphate mannose (DPM) synthase complex; tethers catalytic subunit DPM1 to the endoplasmic reticulum.
|
Q9P2X0
|
A1R7I7
|
COAD_PAEAT
|
Pantetheine-phosphate adenylyltransferase
|
Paenarthrobacter
|
MRRAVCPGSFDPIHNGHLEVIARAAGLFDEVIVAVSTNYAKKYRFSLEDRMEMARETLASLRGIIVEPMGEGLLAEYCRHRGVSAIVKGLRSSSDFDYELPMATMNRQLTGVETVFLPAEAHYVHLSSTLIKEVNVLGGDISEYVPKSVLKRLLAGEPPTEPSRKG
|
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
|
A1R7I7
|
B3LGE9
|
ARO1_YEAS1
|
Shikimate dehydrogenase
|
Saccharomyces
|
MVQLAKVPILGNDIIHVGYNIHDHLVETIIKHCPSSTYVICNDTNLSKVPYYQQLVLEFKASLPEGSRLLTYVVKPGETSKSRETKAQLEDYLLVEGCTRDTVMVAIGGGVIGDMIGFVASTFMRGVRVVQVPTSLLAMVDSSIGGKTAIDTPLGKNFIGAFWQPKFVLVDIKWLETLAKREFINGMAEVIKTACIWNADEFTRLESNASLFLNVVNGEKNVKVTNQLTNEIDEISNTDIEAMLDHTYKLVLESIKVKAEVVSSDERESSLRNLLNFGHSIGHAYEAILTPQALHGECVSIGMVKEAELSRYFGILSPTQVARLSKILVAYGLPVSPDEKWFKELTLHKKTPLDILLKKMSIDKKNEGSKKKVVILESIGKCYGDSAQFVSDEDLRFILTDETLVYPFKDIPADQQKVVIPPGSKSISNRALILAALGEGQCKIKNLLHSDDTKHMLTAVHELKGATISWEDNGETVVVEGHGGSTLSACADPLYLGNAGTASRFLTSLAALVNSTPSQKYIVLTGNARMQQRPIAPLVDSLRANGTKIEYLNNEGSLPIKVYTDSVFKGGRIELAATVSSQYVSSILMCAPYAEEPVTLALVGGKPISKLYVDMTIKMMEKFGINVETSTTEPYTYYIPKGHYINPSEYVIESDASSATYPLAFAAMTGTTVTVPNIGFESLQGDARFARDVLKPMGCKITQTATSTTVSGPPVGTLKPLKHVDMEPMTDAFLTACVVAAISHDSDPNSANTTTIEGIANQRVKECNRILAMATELAKFGVKTTELPDGIQVHGLNSIKDLKVPSDSSGPVGVCTYDDHRVAMSFSLLAGMVNSQNERDEVANPVRILERHCTGKTWPGWWDVLHSELGAKLDGAEPLECTSKKNSKKSVVIIGMRAAGKTTISKWCASALGYKLVDLDELFEQQHNNQSVKQFVVENGWEKFREEETRIFKEVIQNYGDDGYVFSTGGGIVESAESRKALKDFASSGGYVLHLHRDIEETIVFLQSDPSRPAYVEEIREVWNRREGWYKECSNFSFFAPHCSAEAEFQALRRSFSKYIATITGVREIEIPSGRSAFVCLTFDDLTEQTENLTPICYGCEAVEVRVDHLANYSADFVSKQLSILRKATDSIPIIFTVRTMKQGGNFLDEEFKTLRELYDIALKNGVEFLDLELTLPTDIQYEVINKRGNTKIIGSHHDFQGLYSWDDAEWENRFNQALTLDVDVVKFVGTAVNFEDNLRLEHFRDTHKNKPLIAVNMTSKGSISRVLNNVLTPVTSDLLPNSAAPGQLTVAQINKMYTSMGGIEPKELFVVGKPIGHSRSPILHNTGYEILGLPHKFDKFETGSAQLVKEKLLDGNKNFGGAAVTIPLKLDIMQYMDELTDAAKVIGAVNTVIPLGNKKFKGDNTDWLGIRNALINNGVPEYVGHTAGLVIGAGGTSRAALYALHSLGCKKIFIINRTTSKLKPLIESLPSEFNIIGIESTKSIEEIKEHVGVAVSCVPADKPLDDELLSKLERFLVKGAHAAFVPTLLEAAYKPSVTPVMTISQDKYQWHVVPGSQMLVHQGVAQFEKWTGFKGPFKAIFDAVTKE
|
The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis.
|
B3LGE9
|
A4X3K9
|
SSRP_SALTO
|
Small protein B
|
Salinispora
|
MPREKGRKVVASNRKARHDYSILDTYEAGMALTGTEVKSLRAGRASLVDAFAQERNGELYLHGMHIPEYVQGTWTNHEPRRTRKLLLNRIEIDRLIGKTRESGLTIVPLQVYFSDGWAKVEIGVAKGKKSYDKRQDLAKRDAQREIARAAGRRGKGMAD
|
Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation.
|
A4X3K9
|
B8HMJ9
|
GLO2_CYAP4
|
Glyoxalase II
|
unclassified Cyanothece
|
MQIDRLPVLSDNYIFLVLDPERRQAAVVDPAVAAPVLERLRSLQFQLVAIFNTHHHHDHVGGNQELLQHFPTAVVYGGAEDRGRIPGQQVFLQPGDRVNFAQRTAEVLFVPGHTRAHIAYYFPPVNHSSGELFCGDTLFAGGCGRLFEGTPAQMVNSLNQLRQLPDNTRVWCAHEYTLKNLQFALTIEPENVELQTRLAQVYLARQHFQPTVPSELGLEKRTNPFLRWDVPQVQQSVKGQDGIQTFTRLRGRKDQF
|
Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
|
B8HMJ9
|
A2RCQ8
|
MUTS2_STRPG
|
Endonuclease MutS2
|
Streptococcus
|
MNNKILEQLEFNKVKELLLPYLKTEQSQEELLELEPMTEASKIEKSFNEISDMEQIFVEHHSFGIVSLSSISESLKRLELSADLNIQELLAIKKVLQSSSDMIHFYSDLDNVSFQSLDRLFENLEQFPNLQGSFQAINDGGFLEHFASPELERIRRQLTNSERRVRQILQDMLKEKAELLSENLIASRSGRSVLPVKNTYRNRISGVVHDISSSGSTVYIEPRAVVTLNEEITQLRADERHEEGRILHAFSDLLRPHVATIRNNAWILGHLDFVRAKYLFMSDNKATIPKISNDSTLALINVRHPLLSNPVANDLHFDHDLTAIVITGPNTGGKTIMLKTLGLAQLMGQSGLPVLADKGSKIAVFNNIFADIGDEQSIEQSLSTFSSHMTHIVSILNEADHNSLVLFDELGAGTDPQEGASLAMAILEHLRLSHIKTMATTHYPELKAYGIETNFVENASMEFDAETLSPTYRFMQGVPGRSNAFEIASRLGLAPFIVKQAKQMTDSDSDVNRIIEQLEAQTLETRRRLDHIKEVEQENLKFNRAVKKLYNEFSHERDKELEKIYQEAQEIVDMALNESDTILKKLNDKSQLKPHEIIDAKAQIKKLAPQVDLSKNKVLNKAKKIKAARAPRIGDDIIVTSYGQRGTLTSQLKDGRWEAQVGIIKMTLTHDEFTLVRVQEEQKVKNKQINVVKKADSSGPRARLDLRGKRYEEAMQELDHFIDQALLNNMGQVDIIHGIGTGVIREGVTKYLRRHKHVKHFAYAPQNAGGSGATIVTLG
|
Endonuclease that is involved in the suppression of homologous recombination and may therefore have a key role in the control of bacterial genetic diversity.
|
A2RCQ8
|
B3PXA9
|
UREF_RHIE6
|
Urease accessory protein UreF
|
Rhizobium
|
MTGDRELQALLRLTAWLSPAFPIGGFAYSGGLERATADGLVIDAASLAAWIATLISHGSVWNDAVLLAESHRQQPSPAFLAEITALAEALAGSRERHQETMLLGDAFVAAARAWPDEVFERLPGKTAYPVAVGAVAGAHGIGLEKVLVAFLHAYASQAVSSGIRLGVAGQRDGVAVLAGLEEHIVEVARRAAASTLDELGSATVQADIASLRHETQTTRLFRS
|
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
|
B3PXA9
|
Q9BYP8
|
KR171_HUMAN
|
Keratin-associated protein 16.1
|
Homo
|
MGCCPGDCFTCCTQEQNCCEECCCQPGCCGCCGSCCGCGGSGCGGSGCGGSCCGSSCCGSGCGGCGGCGGCGGGCCGSSCCGSSCCGSGCCGPVCCQPTPICDTK
|
In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
|
Q9BYP8
|
P26274
|
LHB_ROSDO
|
Antenna pigment protein beta chain
|
Roseobacter
|
MADNTDLSFTGLTDEQAQELHSVYMSGLFLFAAVAVVAHLATYIWRPWFG
|
Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
|
P26274
|
Q9TIR3
|
MATK_OROFA
|
Intron maturase
|
Aphyllon
|
MEEIKKYLKLEISQQRNFIYPLIFQEYIYAFAYDRGFSRSILILSENLGYDNKSSLLLVKHLITRIYQHNYFIIAPDDSNPNPFWVCSKNFFYEIILEGFAFIVEIPFSLKLISCLEEKNKKIVKYQNLRSVHSIFPFLEDNFSHLNCLFDILIPHFVHTEILVQTFRYCITDVSFLHLLRFFLYKYCKWNSLMTPKKASYSFSKSNQRLLLLLFNIHVYEYESFFVFLHNHSSHLRSIHFEVLLERIHFYGKMECLINIFIKLKDFHANLWLVNESCIHYIRYQRKLIMASKGTSFFMNKWKFYFITFWQCYFSLWFYTRRIYINQSSNHSFEFFGYLSSLRMNPSVVRSQIIENSFLINNIIKKVDTLVSIIPLISSLAKAKFCNVLGHPTSKPIWADLSDYNIIDRFGCICRNLFHYHSGSSKKKFLYRIKYILRLSCARTLARKHKTTVRTFFKIFGSELLEEFLMPEEYVFFFTLSKASCSLQGVYISRIWYLDIISINNLTNYK
|
Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns.
|
Q9TIR3
|
A7ZV06
|
CUTA_ECO24
|
Divalent-cation tolerance protein CutA
|
Escherichia
|
MLDEKSSNTASVVVLCTAPDEATAQDLAAKVLAEKLAACATLIPGATSLYYWEGKLEQEYEVQMILKTTVSHQQALLECLKSHHPYQTPELLVLPVTHGDTDYLSWLNASLR
|
Involved in resistance toward heavy metals.
|
A7ZV06
|
Q0UN58
|
PSF1_PHANO
|
DNA replication complex GINS protein PSF1
|
Parastagonospora
|
MYGETANKLVQNAKRTQALPHLPPYASDLSRTIVREVRDLDRDVSAILAPYGSSFNPSADPSTACALLVNHLCMRRNKRCLLAYHKVRTEKLEGYCWEGIDILEQTGSGKEGEGGMAGKKEESSLSPEEEEYVRQYSDLLAAYKGQWTDIDLTGSLEPPRDLFIDVRVLKDAGEIQTEYGSITLTKNSQFYVRHGDVERLIAQGYLQRLS
|
The GINS complex plays an essential role in the initiation of DNA replication.
|
Q0UN58
|
P13279
|
FER_STRGR
|
Ferredoxin
|
Streptomyces
|
TYVIAQPCVDVKDKACIEECPVDCIYEGQRSLYIHPDECVDCGACEPVCPVEAIFYEDDTPEEWKDYYKANVEFFDDLGSPGGASKLGLIERDHPFVAGLPPQNA
|
Putative electron transport protein for the cytochrome P-450SOY system from the same organism.
|
P13279
|
Q8GIT3
|
NDHO_SYNE7
|
NDH-O
|
Synechococcus
|
MAAALKKGSLVRAIAEQLQGSVELLASDGRIPSYVLETNGEILDIKGDYALVRFSRPTPNVWLRLDQLQSAA
|
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic 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. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
|
Q8GIT3
|
F8P1W3
|
NPS3_SERL9
|
Nonribosomal peptide synthase-like enzyme 3
|
Serpula
|
MAPAPTSVPLVSQPNVISDLKTALAVQGSASDHPRTLHQLLSQAAERYPLQQLGFISSSAHDSSIQTKSYSTFNQHVRNLARALTDWKKPVGSIVVVYLTEHEDNMAAVWACLLAGYIPCLQPALSAQQSHKEGHINHIKNLFLSATWLTNEIGAEQVMSVDGIDIHLFSDLKLAAEGYNVPADWAAVEAKPDDEAILFLTSGSTGFSKAVVHTHRTIIASCYAKGQSYGLTSETNVLNWVGFDHVAGSLEMHITPLLFGSYQLHVHASTILSDPLSFLRLIDDKSINIAFAPNFLLAKLARDLEKRSELYGAFDLSSVKRINSGGEAVVSKTAKIFVTVLKALAKDPSKVSFVVSAGFGMTETCAGCIYDPIDLSVINPMHEFLDLGRPIQGCEMRIVDPEDGITLRPDGESGELQVRGPMVFARYYNNPQATSSSFVEGRWYRTGDIGIIEKGVMRLSGRIKDTVIVHGVSYGIPELETYLQLVEGVTHSFLAAAPYRAPGQETEGFVVFYSPTFDLNEEDASNKLAATHRALRDISVKMITLPPQQIIPIPIDQMEKTTLGKLSRARLLTLFKQGELAKHIARADELLSEARGATFVVPATITETAFAKIFAGVFNLSTDDISAADNFFELGGTSIDVIRLKREGETVFGLPEIPIIQILKHPVLRDLAKYIDALVSKDNTQQEYDPIVPLQLTGNKTPIFFVHPGVGEVLIFVNLAKYFQNERPFYAFRARGFEPGQPFFSKMDEMVSSYAAAMKRTQPKGPYAIAGYSYGGVIAFEVAKRLEAGGDEVKFVGLINIPPHIADRMHEIDWTGGMLNLSYFLGLVSKQDADDLAPTLRPLTRKEQLDVVWKLSPPERLVELQLTPEKLDHWVDIAGSLIECGKDYNPSGSVAVADVFYAIPLRGSKSDWLNNQLKPWSGFSRTEPAFTDVPGRHYTLMDFDHVPQFQKIFRSRLEARGV
|
An L-tyrosine:2-oxoglutarate aminotransferase (probably amt1) and atromentin synthetase nps3 catalyze consecutive steps to turn over L-tyrosine into atromentin, which represents the generic precursor molecule for the entire terphenylquinone and pulvinic acid family of pigments, which are widely distributed secondary metabolites in homobasidiomycetes. The first step catalyzed by the aminotransferase converts L-tyrosine in to 4-hydroxyphenylpyruvate (4-HPP). Adenylation of two 4-HPP monomers by the nps3 adenylation (A) domain, covalent tethering of the monomers as a thioester and oxoester onto the nps3 thiolation (T) and thioesterase (TE) domains, respectively, and symmetric C-C-bond formation between two monomers catalyzed by the nps3 TE domain leads to atromentin. Follow-up products of atromentin in S.lacrymans include atromentic acid, xerocomic acid, isoxerocomic acid and variegatic acid.
|
F8P1W3
|
Q8ZBK0
|
CUEO_YERPE
|
Cuprous oxidase
|
Yersinia
|
MHRRDFLKLTAALGAATSLPLWSRAALAADFSPLPIPPLLQPDANGKINLNIQTGSVVWLPSTATQTWGYNGNLLGPAIRLQRGKAVTIDITNALPEATTVHWHGLEIPGEVDGGPQALIQPGAKRQVTFAVEQPAATCWFHPHTHSKTGHQVAMGLGGLVLIDDSDSETLPLPKQWGVDDIPVILQDKLLDKHGQVDYQLDVMTAAVGWFGDRMLTNGVPYPQQITPRGWVRLRLLNGCNARSLNLALSDGRPMYVIASDGGLLAEPVVVRELPILMGERFEVLVDTRDGQSLDLVTLPVTQMGMTLAPFDQPLPVLRIQPSLAIGSQVLPESLVVIPELADVTGVQERWFQLMMDPKLDMLGMQALVARYGMKAMAGMNMNHGDMGAMDHGNRPDMSQGKMKGMDHGTMNGAPAFNFSHANRINGKAFSMTEPAFDAKQGKYEKWTISGEGDMMLHPFHVHGTQFRILTENGKPPAEHRRGWKDIVRVEGARSEILVRFNYLAPASTPYMAHCHLLEHEDTGMMLGFTVSA
|
Multicopper oxidase involved in copper homeostasis and copper tolerance under aerobic conditions. Is responsible for the oxidation of Cu(+) to the less harmful Cu(2+) in the periplasm, thereby preventing Cu(+) from entering the cytoplasm.
|
Q8ZBK0
|
B2UYB4
|
RS19_CLOBA
|
30S ribosomal protein S19
|
Clostridium
|
MSRSTKKAPFVHEGLLKKIEEMNASGDKKVVKTWSRSSTIYPQMIGHTIAVHDGRKHVPVYLSEDMVGHKLGEFVLTRTYRGHVADKTSKRK
|
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
|
B2UYB4
|
Q63598
|
PLST_RAT
|
T-plastin
|
Rattus
|
MDEMATTQISKDELDELKEAFAKVDLNSNGFICDYELHELFKEANMPLPGYKVREIIQKLMLDGDRNKDGKISFNEFVYIFQEVKSSDIAKTFRKAINRKEGICALGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELSRNEALAALLRDGETLEELMKLSPEELLLRWANFHLENSGWQKINNFSADIKDSKAYFHLLNQIAPKGQKEGEPRIDINMSGFNETDDLKRAESMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFNKYPALTKPENQDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLYVDLQDALVILQLYERIKVPVDWSKVNKPPYPKLGANMKKLENCNYAVELGKNQAKFSLVGIGGQDLNDGNPTLTLAVVWQLMRRYTLNVMEDLGEGQKATDDIIVNWVNGTLSEAGKSTSIQSFKDKTISSSLAVVDLIDAIQPGCINYDLVKTGNLTEEDKHNNAKYAVSMARRIGARVYALPEDLVEVKPKMVMTVFACLMGRGMKSV
|
Actin-bundling protein.
|
Q63598
|
Q5YLB5
|
GYRA_NICBE
|
DNA gyrase subunit A, chloroplastic/mitochondrial
|
Nicotiana
|
MKLHTLNPQTPLTQSKPMAFSTGITPSRFSGLRKTSSELRFLSSVTPPPRKQLRPVSARRKEEEVGDEGNGSVILRDRGENEDRNGGERVVLTELHKEATEAYMSYAMSVLLGRALPDVRDGLKPVHRRILYAMHELGLSSKKPYKKCARVVGEVLGKFHPHGDTAVYDSLVRMAQDFSLRSPLIRGHGNFGSIDADPPAAMRYTECRLEALTESMLLADLEQNTVDFVPNFDNSQKEPSLLPARVPNLLLNGASGIAVGMATNIPPHNLGELVDALSALIHNPEATLQELLEYMPGPDFPTGGIIMGNIGILEAFRTGRGRVVIRGKTDIELLDSKTKRAAIIIQEIPYQTNKASLVEKIADLVENKILEGVSDIRDESDRSGMRIVIELKRGSDPAIVLNNLYRLTALQSSFSCNMVGILNGQPKLMGLKELLQAFLDFRCSVVERRARFKLSQAQERNHIVEGIIVGLDNLDEVINTIRKASSNALAAASLRKEFELSEKQAEAILDISLRRLTALERNKFVEEGKSLRTQISKLEELLSSKKQILQLIEEEAIEIKNKFFNPRRSMLEDTDSGDLEDIDVIPNEEMLLAISEKGYVKRMKPDTFNLQNRGTIGKSVGKLRVNDAMSDFLVCRAHDKVLYFSDKGTVYSSPAYKIPECSRTAAGTPLVQILSLSDGERITSIIPVSEFAADQYLVMLTVNGYIKKVSLNYFASIRCTGIIAIQLVPDDELKWVKCCSNNDFVAMASQNGMVILTPCANIRALGRNTRGSVAMRLKEGDKVASMDIIPDALQKELDKTLEVQQRQYRSMKGPWLLFVSESGYGKRVPVSRFRTSPLNRVGLFGYKFSSEDCLAAVFVVGFSLGEDGESDEQVVLVSQSGTVNRIKVRDISIQSRYARGVILMRLEHAGKIQSASLISAADADPEDEDATAVAA
|
A type II topoisomerase that seems to play a critical role in chloroplast nucleoid partitioning by regulating DNA topology. DNA gyrase negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner.
|
Q5YLB5
|
Q1D7U5
|
RL10_MYXXD
|
50S ribosomal protein L10
|
Myxococcus
|
MLKSEKEEMIKELHEKFSRTTSAVVAEFTKVDVETVTKLRKKFREGNVEYKVIKNTLARRAAQGTSVSVIADDFTGPVALCISYGDVVAPAKILVEFAKDIEDKIKIRTAVVEGRKVDVAGVKALAKLPGLPELRAQLLGVISEPASKLVRTIAAPGSQLARVVQANADKAQG
|
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
|
Q1D7U5
|
Q9ZR79
|
LRK57_ARATH
|
L-type lectin-domain containing receptor kinase V.7
|
Arabidopsis
|
MSHKVLQIVLVLLLTLFSSTHNSNGNFLMEEAAAAGLNGYCLLTNTTKHSYGQAFNNTPVPIKNSSFSFNIIFGIVPEHKQQGSHGMAFVFSPTRGLPGASPDQYLGIFNETNNGKASNNVIAIELDIRKDEEFGDIDDNHVGININGLTSVASASAGYYDDEDGNFKKLSLISTKVMRLSIVYSHTDKQLNVTLLPAEISVPPQKSLLSLNRDLSPYFLEETYLGFTASTGSIGALYYVMQFSYEEGVIYPAWDLGVIPTLPPYPKKSYDRTRRILAVCLTLAVFTALVASGIGFVFYVRHKKVKEVLEEWEIQNGPHRFSYKELFNATKGFKEKQLLGKGGFGQVYKGMLPGSDAEIAVKRTSHDSRQGMSEFLAEISTIGRLRHPNLVRLLGYCKHKENLYLVYDFMPNGSLDRCLTRSNTNENQERLTWEQRFKIIKDVATALLHLHQEWVQVIVHRDIKPANVLLDHGMNARLGDFGLAKLYDQGFDPQTSRVAGTLGYIAPELLRTGRATTSTDVYAFGLVMLEVVCGRRLIERRAAENEAVLVDWILELWESGKLFDAAEESIRQEQNRGEIELVLKLGLLCAHHTELIRPNMSAVLQILNGVSHLPNNLLDVVRAERLRGIPETSMEVLLGLDLNSFGTMTLTNSFVSHGR
|
Involved in resistance response to the pathogenic oomycetes Phytophthora infestans and Phytophthora capsici and to the pathogenic bacteria Pseudomonas syringae.
|
Q9ZR79
|
Q9SL29
|
CNG15_ARATH
|
Cyclic nucleotide- and calmodulin-regulated ion channel 15
|
Arabidopsis
|
MGYGNSRSVRFQEDQEVVHGGESGVKLKFKINGTQINNVKMMSKGKFLKAKVLSRVFSEDLERVKTKILDPRGQTIRRWNKIFLIACLVSLFVDPLFFFLPVMRNEACITIGVRLEVVLTLIRSLADAFYIAQILIRFRTAYIAPPSRVFGRGELVIDSRKIAWRYLHKSFWIHLVAALPLPQVLIWIIIPNLRGSPMTNTKNVLRFIIIFQYVPRMFLIFPLSRQIIKATGVVTETAWAGAAYNLMLYMLASHVLGACWYLLAVERQEACWRHACNIEKQICQYRFFECRRLEDPQRNSWFEWSNITTICKPASKFYEFGIFGDAVTSTVTSSKFINKYFYCLWWGLKNLSSLGQNLATSTYAGEILFAIIIATLGLVLFALLIGNMQTYLQSTTMRLEEWRIRRTDTEQWMHHRQLPPELRQAVRKYDQYKWLATRGVDEEALLISLPLDLRRDIKRHLCFDLVRRVPLFDQMDERMLDAICERLKPALCTEGTFLVREGDPVNEMLFIIRGHLDSYTTNGGRTGFFNSCLIGPGDFCGEELLTWALDPRPVVILPSSTRTVKAICEVEAFALKAEDLQFVASQFRRLHTKQLRHKFRFYSHQWRTWAACFIQAAWRRHRKRKYKTELRAKEEFHYRFEAATARLAVNGGKYTRSGSDSGMMSSIQKPVEPDFSSE
|
Putative cyclic nucleotide-gated ion channel.
|
Q9SL29
|
A5W4F2
|
BNZA_PSEP1
|
Toluene 2,3-dioxygenase subunit alpha
|
Pseudomonas
|
MNQTDTSPIRLRRSWNTSEIEALFDEHAGRIDPRIYTDEDLYQLELERVFARSWLLLGHETQIRKPGDYITTYMGEDPVVVVRQKDASIAVFLNQCRHRGMRICRADAGNAKAFTCSYHGWAYDTAGNLVNVPYEAESFACLNKKEWSPLKARVETYKGLIFANWDENAVDLDTYLGEAKFYMDHMLDRTEAGTEAIPGVQKWVIPCNWKFAAEQFCSDMYHAGTTSHLSGILAGLPEDLEMADLAPPTVGKQYRASWGGHGSGFYVGDPNLMLAIMGPKVTSYWTEGPASEKAAERLGSVERGSKLMVEHMTVFPTCSFLPGINTVRTWHPRGPNEVEVWAFTVVDADAPDDIKEEFRRQTLRTFSAGGVFEQDDGENWVEIQHILRGHKARSRPFNAEMSMDQTVDNDPVYPGRISNNVYSEEAARGLYAHWLRMMTSPDWDALKATR
|
Catalyzes both the oxidation of benzene and toluene.
|
A5W4F2
|
Q8NZF8
|
PYRG_STRP8
|
UTP--ammonia ligase
|
Streptococcus
|
MTKYIFVTGGVVSSIGKGIVAASLGRLLKNRGLKVTIQKFDPYINIDPGTMSPYQHGEVYVTDDGAETDLDLGHYERFIDINLNKYSNVTTGKIYSEVLRKERKGEYLGATVQVIPHITDALKEKIKRAASTTDSDVIITEVGGTVGDIESLPFLEALRQMKADVGSENVMYIHTTLLPYLKAAGEMKTKPTQHSVKELRGLGIQPNMLVIRTEEPVEQGIKNKLAQFCDVNSEAVIESRDVEHLYQIPLNLQAQSMDQIVCDHLKLNAPQADMTEWSAMVDKVMNLRKTTKIALVGKYVELPDAYLSVVEALKHSGYANDTAIDLKWVNANDVTVENAADLLGDADGIIVPGGFGQRGTEGKIQAIRYARENDVPMLGICLGMQLTCVEFARHVLNMEGANSFELEPSTKYPIIDIMRDQIDIEDMGGTLRLGLYPCKLKPGSKAAMAYNNQEVVQRRHRHRYEFNNKFRSEFEAAGFVFSGVSPDNRLVEIVELKEKKFFVAAQYHPELQSRPNRPEELYTAFVTAAIKNSN
|
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
|
Q8NZF8
|
B7UQX7
|
SYME_ECO27
|
Endoribonuclease SymE
|
Escherichia
|
MTDTHSIAQPFEAEVSPANNRQLTVSYASRYPDYSRIPAITLKGQWLETAGFATGTAVDVKVMEGCIVLTAQPPAAEESELMQSLRQVCKLSARKQKQVQEFIGVISSKTPR
|
Involved in the degradation and recycling of damaged RNA. It is itself a target for degradation by the ATP-dependent protease Lon.
|
B7UQX7
|
Q28399
|
ALDH1_ELEED
|
ETA-crystallin
|
Elephantulus
|
MSSSGMPDLPAPLTNIKIQHTKLFINNEWHESVSGKTFPVFNPATEEKICEVEEADKEDVDKAVKAAREAFQMGSPWRTMDASERGQLIYKLADLIERDRLLLATLESINAGKVFASAYLMDLDYCIKALRYCAGWADKIQGRTIPVDGEFFSYTRHEPIGVCGLIFPWNAPMILLACKIGPALCCGNTVIVKPAEQTPLTALHVASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDVDKVAFTGSTEVGKMIQEAAAKSNLKRVTLELGAKNPCIVFADADLDSAVEFAHQGVFTNQGQSCIAASKLFVEEAIYDEFVQRSVERAKKYVFGNPLTPGVNHGPQINKAQHNKIMELIESGKKEGAKLECGGGPWGNKGYFIQPTVFSNVTDDMRIAKEEIFGPVQQIMKFKSLDEVIKRANNTYYGLVAGVFTKDLDKAVTVSSALQAGTVWVNCYLAASAQSPAGGFKMSGHGREMGEYGIHEYTEVKTVTMKISEKNS
|
Major component of the eye of elephant shrews, which in contrast to other mammals, possesses both a lens- and a non-lens class-1 aldehyde dehydrogenase 1. This eye-specific form is a structural protein of the lens and, in other part of the eye, serves as the major form of ALDH1. Can convert/oxidize retinaldehyde to retinoic acid.
|
Q28399
|
A9SMC8
|
THI44_PHYPA
|
Thiazole biosynthetic enzyme 4
|
Physcomitrium
|
MSSQAGNVGSSSSSLAGVRMVVSPKAQLRHARLPAASASMYSDAKYDLNNYKFEPIKESIVAREMTRRYMTEMITHADTDVVVVGAGSAGLSCAYELSKNPNVKVAIIEQSVSPGGGAWLGGQLFSAMVVRKPAHRFLDEIEVPYEELENYVVIKHAALFTSTIMSKLLARPNVKLFNAVAAEDLIIRGDRVSGVVTNWALVAQNHNTQSCMDPNVMEAKVVVSSCGHDGPFGATGVKRLRSIGMIESVPGMKCLDMNAAEDAIVKHTREVVPGMIVTGMEVAEIDGSPRMGPTFGAMMISGQKAAHLALKALGLPNELDGNYKLNVHPELVLASTDDETASA
|
Involved in biosynthesis of the thiamine precursor thiazole. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an adenylated thiazole intermediate. The reaction includes an iron-dependent sulfide transfer from a conserved cysteine residue of the protein to a thiazole intermediate. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. May have additional roles in adaptation to various stress conditions and in DNA damage tolerance.
|
A9SMC8
|
Q3IU15
|
PCNA_NATPD
|
Proliferating cell nuclear antigen homolog
|
Natronomonas
|
MFKAIVSADTLGAALDSVSVLVDECKVRLDEEGLTIRAVDPANVGMVDLELSASAFESYETDGGVIGVNLDRLEDIVGMADSGQLVHLDLDEETRKLHISLDGLEYTLALIDPDSIRQEPDLPDLDLSSEIVIEGADIDRAVTAADMVSDHIALGVDPDAEEFYVDAEGDTDDVHLELDREDLIDLTPGEARSLFSLDYLKDMNKAIPKDAEVTMELGEEFPVKMHFDFAEGDGHVTYMLAPRIQSD
|
Sliding clamp subunit that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase and other proteins to DNA during high-speed replication.
|
Q3IU15
|
B4SJT8
|
HEM3_STRM5
|
Pre-uroporphyrinogen synthase
|
Stenotrophomonas maltophilia group
|
METVRIATRKSPLALWQSEHVADRLRQAHPGLHVELVPMSTRGDEVLDRSLAAIGGKGLFLKELELAMLRGEADCAVHSLKDVPMELDEPFALPAMLTRHDPADGFVSNLYASLDALPIGARVGTSSLRRQAQLRALRPDLQLLDLRGNVNTRLAKLDNGGYDAIVLAVAGLERLGLGERIVARLQPPQWLPAPAQGAVAVECDGSNARLMALFAGLDDAATRACVEAERAMNRALHGSCHVPVAAIAQWQGQDLHLQGLVGSASDGRAVRAEAVGPASDPEVLGQRVAKMLLDAGAGELLNV
|
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
|
B4SJT8
|
Q3KRA9
|
ALKB6_HUMAN
|
Alkylated DNA repair protein alkB homolog 6
|
Homo
|
MEEQDARVPALEPFRVEQAPPVIYYVPDFISKEEEEYLLRQVFNAPKPKWTQLSGRKLQNWGGLPHPRGMVPERLPPWLQRYVDKVSNLSLFGGLPANHVLVNQYLPGEGIMPHEDGPLYYPTVSTISLGSHTVLDFYEPRRPEDDDPTEQPRPPPRPTTSLLLEPRSLLVLRGPAYTRLLHGIAAARVDALDAASSPPNAAACPSARPGACLVRGTRVSLTIRRVPRVLRAGLLLGK
|
Probable dioxygenase that requires molecular oxygen, alpha-ketoglutarate and iron.
|
Q3KRA9
|
A6TT61
|
BIOB_ALKMQ
|
Biotin synthase
|
Alkaliphilus
|
MDIKKLPKEIIEGRRLKREEDLRFFATANLEELCQGADNIRKVLCGDAVNLCSIINGKSGKCSENCKFCAQSSHHHTGIEEYSFLDTNLIVEDCKKHANKGVHRYSIVTAGRELKGKDLQVACDAYKRMKEECDIDLCASHGLLSEEAFIALKESGVSMYHENIETSKRNFPNICTTHTYKDKINAIKLAQRLGFKVCSGGIIGMGETFEDRLDMAVSLAELKIQSIPINTLMPIKGTTYEDLEPLTEDEILRTVAMFRFINPTANIRLAAGRSLMEDSGRRAFHAGANATITGDLLTTSGNNIDKDKEMLTQMGFHL
|
Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
|
A6TT61
|
Q5FPK0
|
COAE_GLUOX
|
Dephosphocoenzyme A kinase
|
Gluconobacter
|
MKIIGLTGGMAAGKSTVAALFRREGVPVFDADACVRALQGERGKALPLIGQAFPGTVVASRLDRAALREAVRGRPEALQRLEAIMHPLVRVERERFLKQCRARHEPFCVLDIPLLMEIGEDRRCDVVMVAEAPMGTRLARIRQRGRSGGRMSLADAKGLLARQMSDHERRRRADIVIRTGLSRGQAVRQVHALLHRLREAS
|
Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
|
Q5FPK0
|
A1W2F6
|
ALR_ACISJ
|
Alanine racemase
|
unclassified Acidovorax
|
MPRPILATIHPAAVHHNLERARRAAPDARVWAVVKANAYGHGIERVFEGLRAADGFALLDLAEAERVRALGWRGPILLLEGVFEPRDLELCSRLGLWHAVHCDAQIDWLAAHKTQVPHRVFLKMNSGMNRLGFTPERYRSAWARLNALPQVDEISCMTHFSDADGPRGIAHQVQAFQAATQDLPGERCIANSAALLRHGGDAQVRLDWVRAGIVLYGSAPDHPERRAADWDLQPTMTLASRIIGVQQLQAGDTVGYGSRFTAQGPLGIGIVACGYADGYPRHCDTGTPVLVNGVRTRTIGRVSMDMLAVDLTPVPGAGLGAEVTLWGRAANGAVLPIDEVAQAGGTIGYELMCALAPRVPVVVQD
|
Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
|
A1W2F6
|
B1Z772
|
KAD_METPB
|
Adenylate monophosphate kinase
|
Methylorubrum
|
MRIILLGPPGAGKGTQSERIVERYRVPQLSTGDMLRAAVAAGTPVGLEAKSIMESGGLVPDAVVVGIVADRIEEADARDGFILDGFPRTVEQAKALDAMLAEKGIALDAVVEFVVDENALVGRIAKRAEETAARGQPVRKDDTPEVFKTRLDAYKRQTAPLSDYYAGTGLLRKIDGMKPIDEVTGDVTGLLDGFREKATS
|
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
|
B1Z772
|
B7KAA8
|
PDXA_GLOC7
|
4-(phosphohydroxy)-L-threonine dehydrogenase
|
Gloeothece citriformis
|
MKSLALTLGDPAGIGSEVILKALADPSVGENYNITVVGSRSLLEESYHQLRSLPHVNHSDLVDPANLLILDIPLDKTTKSQIQLGKGNAASGEASFTYLQAAIAGTLKGEFAGIVTAPIAKSCWKAAGYHYPGQTEVLAQAAGVEKFGMLFVARSPYTGWMLRTLLATTHIPLSQVPTVLTPELMTLKLELLIDCLKNDFRLDHPKIAIAGLNPHSGEQGQLGTEERDWLTPWLEEEKKRHCEVELVGLVPPDTMWVTPGQAWYGNAPHPQHGADGYLALYHDQGLIPVKLMAFDQAINTTIGLPFIRTSPDHGTAFDIAGKGIARPASMIEAIKLAQALVNG
|
Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
|
B7KAA8
|
B4S5A3
|
RS11_PROA2
|
30S ribosomal protein S11
|
Prosthecochloris
|
MATISRKKKKVKVTPEGAVHIKASFNNVLVTITDMQGNTVSWSSAGKNGFKGSKKNTPYASQVTSEAAAKEAFDLGMRYVHVFIKGPGSGRDAAIRALQGAGLDVKTIKDITPLPHNGCRPPKRRRV
|
Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome.
|
B4S5A3
|
C1C6H0
|
DEOD_STRP7
|
Purine nucleoside phosphorylase DeoD-type
|
Streptococcus
|
MSIHIAAQQGEIADKILLPGDPLRAKFIAENFLGDAVCFNEVRNMFGYTGTYKGHRVSVMGTGMGMPSISIYARELIVDYGVKKLIRVGTAGSLNEEVHVRELVLAQAAATNSNIVRNDWPQYDFPQIASFDLLDKAYHIAKELGMTTHVGNVLSSDVFYSNYFEKNIELGKWGVKAVEMEAAALYYLAAQYHVDALAIMTISDSLVNPDEDTTAEERQNTFTDMMKVGLETLIAE
|
Catalyzes the reversible phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.
|
C1C6H0
|
B7LTQ3
|
MTFA_ESCF3
|
Mlc titration factor A
|
Escherichia
|
MIKWPWKAQETPQQDNPPWEDALAIPILHSLTTEEQTRLVALAERFLQQKRIVPLQGFELDSLKSARIALLFCLPVLELGIEWLDGFHEVLIYPAPFVVDDEWEDDIGLVHNQRIVQSGQSWQQGPIVLNWVDIRDSFDASGFNLIIHEVAHKLDMRNGDRASGIPLIPLREVAGWEHDLHAAMENIQEEIDLVGETASSIDAYAATDPAECFAVLSEYFFSAPELFAPRFPSLWQRFCQFYGQNPLLRLRNSPNNDASPTTNVH
|
Involved in the regulation of ptsG expression by binding and inactivating Mlc.
|
B7LTQ3
|
Q4W9B9
|
ISN1_ASPFU
|
IMP-specific 5'-nucleotidase 1
|
Aspergillus subgen. Fumigati
|
MTTRYRVEFASSRPTGKFFTARLNGQTNIFQIEWIKGLLAVPFVLHSQPTAVYQEHSENLVAVAADTHQRYAEIFRDVEKLIDDHSRPLAPPPPPVLASHLTLSVDHERNAAPGKSKLKLLVPTAGSFFSRLPLEDAFKYQDAKRMISRRRFVAPSFNDIRLTLNTAQLLGLVRGPGLDLVTFDGDVTLYDDGACLTPDNPAIPRIIRLLHQGVRIGIVTAAGYTEGAKYYERLKGLLDAVHDSSSLTPAQKDGLVVMGGESNFLFRFDSASPHRLSYVPRPEWLLDEMKSWNQEDITQLLDIAESSLRACAANLNLPVAVLRKDRAVGVYPYDRSKIHREQLEETVLVVQNTVERSVVGSRLPFCAFNGGNDVFVDIGDKSWGVRACQRYFGGIEPSRTLHVGDQFLSAGANDFKARLASTTAWIASLTETVQLLDELEEMQKAEKNRS
|
IMP-specific 5'-nucleotidase involved in IMP (inositol monophosphate) degradation.
|
Q4W9B9
|
Q8BQ48
|
CE295_MOUSE
|
Centrosomal protein of 295 kDa
|
Mus
|
MKRKGMNTKLRLSPSEEAFILKEDYERRRKLRLLQVREQERGIAFQIREGIKQRRSQQVSHLAEELRAKWEEAQSQKIQNLEKLYLASLRHMGDGHRQAKENEPDLDALSRRAAERKRKAEVRHKEALKVQKNQKEMLMKQKTRHIKARKEAVLVEKQRSAKMARLPPPVPSPFENIDVNRIPSLKTNSSTYHHISTFVSRQMGTKQPDAHLAAEEEARRVERLRKQAAQERVKQFERAHVRGSQAMKKIHLAQNQERLMEELKQLQKEDLARRRQTVAQMPPQMLELPYRRSEMKEDRQRELEFAFEDMYNADRKVKGNLILHLKPEPLPTISDQLQDEELDLSMEQENQVPLAAKIQQIPSRILFKRLLNKIRSQKSLWTIKSVSEDEGEVTSSIIEIESKVPSVDSGAIITEERTAASFEQEQVTDSDRLTIESGPLSSEDKPLYYKAGTGREQAMAVSPPATAVAQSSVLLHPQEEAVRIRMSLRRKQIMEIEEQKQKQLELLEQIEQQKLRLETDCFRAQLEEQRKQADQPEVCCAPMSHAMISDEDSHRQMIRNYQHQLLQQNRLHKETVETARKRLLEYQTVLKERSPSLSASALVPDSVVSGPPQQSYKPAAASDSWDPSQRLKLSPSKYQPVQPSQIPALEQSHIQVPRHGHITQRQGKMAVSEMLGKQPVESQERQWQFSQVETHQGDYEFVLKDSHSLSRTLSYVRPQTLQDAREVSKPPRVIICQSLDSQQISSEDSENISSKPSEPSPFLPLVPERPFTSLPVKFHSGTIHKPFTTINQSVISQMHDQPLSSSETITAQQGDLRFLQEQLELQKKVLQARQEAREKLLLCTQKELGQQTGLPVFLPSPAGNIFSSLPSASAESGNFQTSSTKSDATVSSDNMDRLWDSSQPISSQQTHLEFLQEQSSVETDNLQARREAQEVLFAHTQNTLEKIVRSEQAGSSLPHQVAQQSFSSLTLADTQSKKIQKQPLPANKKGLLPSQSEVSKAQDGSSGFLQQTLPLQNTLKLLQEQLTRQRSMIPPRRDGQETLLLYKESCSEDSEAGPVESLSSVVVQHADASRAVSEVPKRLQDVYSSEEENRVLSSHLITHGFPQHSLQRQEHFTPLQEETHIQRLILGARKNNEEFAPKQNELEKGLCSQQTDALSSPSQVTDWGTSRGSVSVRSDRTDPLRHFKIPAFRERLVRVSQHTFPLQDNLQEHQEWVDTEKESFQSSPLTPENPSSQQTGFSSFKASLRLPSCVSLPSADSGITQHPLSTESDSKVKSSHLQIPELQHRLSKISQLIPPQQDSLKALQEQLATQREAIIHSRQEAHEETLREWKEKIFPEQVGPFSPLIPQHSLASFPVSDTERAQELCSTNSDTISSGYPEMLELPDRTLGLSHTALPQQNNLTAHPEHLHAQTNFFHSTEKAQEGLVFPRPCQFEEMSAEHFIQPQHDDLKALQQQLDMQREAIRSGQEMQEKMLLQRLNKLEQRISSKQISSSLFSSQVALPIANSDGTLQSFPTKSNETELLGSQDEYLSFSQPRLPLQNNMTEQLDLEKVFHKELLLHKQKSQNKSESSEHSLPPLFLSKEIEHPFISLPFAESKSKSICELYLSDKKHAAPNDAVIPRLQDRLLSCSQPVLTQQDNMSLQKQLNLQRETLHSRQKAQEELLVQRQTSLQQQIQRHRETLKNFFNVSQARNPTDENDLEMQKREQLGGWFPHTQGLTWGDAGQGSANGEQPRADVHAEHNGESLAKELSGRASKPPVSKVKCVLDLNQHELSTIQEVESPASGRISMPGKAEFYQDRDPLRVSVSREQSFLESPLAHDPFGCHQPPAQENSKSHDDNAEAVKVKKSDVEDHAVLSHAVSKEEACTNLGPLGKPDDEAETQEISQEPLSSVTVSTGSFLSYEITDLSLTDPESFSEQTEHLEQESTNKQEETDPLSIAVPSVIYQQQHSLGAHNSLLPMEEESTSDHTHVQQIMDNDVNEANLIPDKRDFQVPAVDLDFRELEHIFPHLHRQLFKPLEPHLDFDLSSPGTSQEDSDFYQSSESSSEKHVKALSTGTICFPALTAKSHSPNPRLNQLDINLAHATTEGSEQSFQQLRPEFSSQESQHADLPSIYSIEARGPSQRMENQNYSEMLQNKKKSLSLQPSTEDLTPACSSSDTALFDQLHLQHSTPCASVSSECSVKLLESREEVLGFEELSRRAVTMSQRLTEDENVVLPINPHVGRVEKEASVQGSNPLSIQNEKPIQNFIETDTTEAVGNVCQLAQAEHILKSCPFRSPIPIWETDTGYGIMEEPDLTLVSNSDISITETDLANLTLEDREDNEAQFFQAGVVLPTSSMETSVCGAVSEPYVDQPTVAPSATSGSLQEAFMTRQTLTERSYQRQREIWNKTRLPQTKVSKEKLPTGCTGS
|
Centriole-enriched microtubule-binding protein involved in centriole biogenesis. Essential for the generation of the distal portion of new-born centrioles in a CENPJ- and CEP120-mediated elongation dependent manner during the cell cycle S/G2 phase after formation of the initiating cartwheel structure. Required for the recruitment of centriolar proteins, such as POC1B, POC5 and CEP135, into the distal portion of centrioles. Also required for centriole-to-centrosome conversion during mitotic progression, but is dispensable for cartwheel removal or centriole disengagement. Binds to and stabilizes centriolar microtubule.
|
Q8BQ48
|
A0DSB3
|
PP2C6_PARTE
|
Probable protein phosphatase 2C 6
|
Paramecium
|
MGPYLSQPKTEKTSVTGQNQVLQYAATHMQGWRNTMEDAHISDLNIEPDVHLFAVFDGHGGSEVAIFAERHFREELMKNKNYQQKNYEKALTETFFKIDKMLQEPSGLDELNKIRGVTDEASLAGCTANVALIVGKTLYVANAGDSRSFLNRDGKPFDMSKDHKPDDEQEKKRIERAGGFVSDGRVNGNLSLSRALGDLEYKKDNRFKPEEQIITALPDVKVTQLSAADKFLLMGCDGVFETWDHQQILNFINSELKNTQNLQKAAEKLLDQLLAKDTSLGTGCDNMTCILIQFK
|
Enzyme with a broad specificity.
|
A0DSB3
|
P49582
|
ACHA7_MOUSE
|
Neuronal acetylcholine receptor subunit alpha-7
|
Mus
|
MCGRRGGIWLALAAALLHVSLQGEFQRRLYKELVKNYNPLERPVANDSQPLTVYFSLSLLQIMDVDEKNQVLTTNIWLQMSWTDHYLQWNMSEYPGVKNVRFPDGQIWKPDILLYNSADERFDATFHTNVLVNASGHCQYLPPGIFKSSCYIDVRWFPFDVQQCKLKFGSWSYGGWSLDLQMQEADISSYIPNGEWDLMGIPGKRNEKFYECCKEPYPDVTYTVTMRRRTLYYGLNLLIPCVLISALALLVFLLPADSGEKISLGITVLLSLTVFMLLVAEIMPATSDSVPLIAQYFASTMIIVGLSVVVTVIVLRYHHHDPDGGKMPKWTRIILLNWCAWFLRMKRPGEDKVRPACQHKPRRCSLASVELSAGAGPPTSNGNLLYIGFRGLEGMHCAPTPDSGVVCGRLACSPTHDEHLMHGTHPSDGDPDLAKILEEVRYIANRFRCQDESEVICSEWKFAACVVDRLCLMAFSVFTIICTIGILMSAPNFVEAVSKDFA
|
After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. The channel is blocked by alpha-bungarotoxin.
|
P49582
|
A4Y2Z8
|
RIMO_SHEPC
|
Ribosome maturation factor RimO
|
Shewanella
|
MTVETFKPKQTTTLDTPAKRLEAASTNAVTTGNRIGFVSLGCPKNLVDSERILTQLRIDGYEVTNSYDNADLVIVNTCGFIDAAVEESLDAVREALEENGKVIVTGCLGAKENQIREVYPDVLEITGPHSYEAVLKHVHKYVPKPEHNPFTSLIPQTGVKLTPKHYAYLKISEGCDNRCTFCIIPSLRGDLNSRPAGSILDEAKRLVESGVQEILVVSQDTSAYGKDKSGRTDFWDGMPVKQDITSLARQLGKMGAWVRLHYIYPYPWVDDLIPLMAEGLILPYLDIPMQHASPRILKMMKRPGRVDRQLEAIQRWREICPDLVIRSTFIVGFPGETEEDFQILLDFLKEARLDRVGCFKYSEVDGAVANTIAELISEDVKEDRYHRFMELQAEISAERLARFVGRTLDILIDDVDEEGAIGRSFADAPEIDGMVFINGETELEPGMLVRARITHSDEHDLWAEVVDADTQD
|
Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12.
|
A4Y2Z8
|
Q4G064
|
COQ5_RAT
|
Ubiquinone biosynthesis methyltransferase COQ5
|
Rattus
|
MAAPRSCVLWSYCGHGWSRLAGDCRLPGFRRSWLGATLSARSLSQEKRAAETHFGFETVSEKEKGGKVYQVFQSVARKYDLMNDMMSLGIHRAWKDLLIRKMHPLPGTQLLDVAGGTGDIAFRFLSYVQTQHERKQRRQLRTRQNLSWEEIARKYQSKEDPLGGSLVMVCDINREMLKVGKQKALARGHTAGLAWVLGDAEELPFDDDRFDVYTIAFGIRNVTHIDRALQEAHRVLKPGGRFLCLEFSQVNDPLISRLYDLYSFQVIPVIGEVIAGDWKSYQYLVESIRKFPNQEEFKDMIEDAGFQKVTYESLTSGIVAIHSGFKL
|
Methyltransferase required for the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
|
Q4G064
|
G0SC29
|
NLE1_CHATD
|
Ribosome biogenesis factor RSA4
|
Thermochaetoides
|
MATLAPPPSKRQRREEIQRTQTQQDVTPLVATDLGSFKANFIDSDGNQMTDVVEINFADATEKNISNLLNTLLGRDREEFTPYRFRIHIPGKDLIIDQYPNDLLSLLQKHGVTNPFETTITLSAEPQAIFKVHAVSRLAHRIPGHGQPILSCQFSPVSSSRLATGSGDNTARIWDTDSGTPKFTLKGHTGWVLGVSWSPDGKYLATCSMDTTVRVWDPESGKQVNQEFRGHAKWVLALAWQPYHLWRDGTARLASASKDCTVRIWLVNTGRTEHVLSGHKGSVSCVKWGGTDLIYTGSHDRSVRVWDAVKGTLVHNFTAHGHWVNHIALSSDHVLRTAYHDHTKEVPGTEEERRAKAKERFEKAAKIKGKVAERLVSASDDFTMYLWDPTNNGSKPVARLLGHQNKVNHVQFSPDGTLIASAGWDNSTKLWNARDGKFIKNLRGHVAPVYQCAWSADSRLVVTGSKDCTLKVWNVRTGKLAMDLPGHEDEVYAVDWAADGELVASGGKDKAVRTWRN
|
Involved in ribosome biogenesis. Required for processing and efficient intra-nuclear transport of pre-60S ribosomal subunits. Interacts with the AAA-ATPase Midasin, which is essential for the ATP-dependent dissociation of a group of nonribosomal factors from the pre-60S particle.
|
G0SC29
|
C0NM08
|
ECM14_AJECG
|
Inactive metallocarboxypeptidase ECM14
|
Histoplasma
|
MRLFTHGQVLALLAFVNTISATPSFSTNSYPAHPAEPVSLFSQHQPQAPLGLWTRLRNSVIERVWGVPPQQRHRGGNKHQYPPFSAPASLRARYGDDVVLRFKLQTADEVKALVEASNILFLDVWSSTDEWIDIRLAKDVVPSLLGLLPKSLQTTHVPLIRDLPQTIYESYPSPSQSPSGRERGFLPSGEPSSDVTNIFFENYQPLSVIVPWMRLLASMFPSHAQFISIGSSFEGRDIPALRVGVRPANDQKPRRTLIIEGGSHAREWIGVSTVNYVAYSLITSYGKSKPISTLLEQFDFIFIPTINPDGYVYTWETDRLWRKNRQETSLPFCPGVDLDRTWGFEWNGNATGDNPCLESYGGDKPFAGVEAHQLAEWVKEQTEQRNTKFVAYMDLHSYSQQILYPYSYSCLYQPPNLENLEELAMGIAKAIRLTNRKTYAVSSACGGLMASQKKKAKPETFLRMESTGGSALDWFYHDFGVKYAYQLKLRDRGSYGFLLPRENIVPTGKEVFNAVMMLGRFLLGESNAFQELDWDAGFQRPKKDDKPILNDDDDDDADTNDDGIGRKDDSWIPDEYKGDNDRDESDGGWAFRRLRKR
|
Inactive carboxypeptidase that may play a role in cell wall organization and biogenesis.
|
C0NM08
|
P23575
|
GRPE_CHLMU
|
HSP-70 cofactor
|
Chlamydia
|
MTETPNTSSEEIQTSEPSSDNELQTLQQENANLKAELKEKNDRYLMALAEAENSRKRLQKERTEMMQYAVENALLDFLPPMESMEKALGFASQTSDEVKNWAIGFQMILQQFKQVFEDKGVVEYSSKGELFNPYLHEAVEIEETTDIPEGTILEEFTKGYKIGDRPIRVAKVKVAKFPTKGNNDSNEEKE
|
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
|
P23575
|
P16851
|
IAAC2_WHEAT
|
Chloroform/methanol-soluble protein CM2
|
Triticum
|
MASKSSITHLLLAAVLVSVFAAAAATGPYCYPGMGLPSNPLEGCREYVAQQTCGVGIVGSPVSTEPGNTPRDRCCKELYDASQHCRCEAVRYFIGRTSDPNSGVLKDLPGCPREPQRDFAKVLVTPGHCNVMTVHNTPYCLGLDI
|
Alpha-amylase/trypsin inhibitor. It could be involved in insect defense mechanisms.
|
P16851
|
Q07182
|
SODC_CHYAM
|
Superoxide dismutase [Cu-Zn]
|
Chymomyza
|
MVAKAVCVINGDAKGTVYFEQEDACAPVKVCGEITGLNKGQHGFHVHEFGDNTNGCMSSGPHFNPLNKEHGAPTDENRHLGDLGNIEAPGDGPTKVCINDSKITLFGENSIVGRTVVVHADPDDLGKGGHELSKSTGNAGARIGCGVIGICKI
|
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
|
Q07182
|
Q9UQW9
|
DCOR_SCHPO
|
Ornithine decarboxylase
|
Schizosaccharomyces
|
MPAIMEKNMLVSESLRTTELLGHVKPIDSVVTWSSPGSSRQAIGEAFKNTIEEIERAAVRGEPADSDAFFVADLNGVYRQLLRWHAKLPRVQPFYAVKCNPDPKVLALLNKFGTGFDCASKGELEQILGLGVSPDRIVYANPCKAITYVRYAASKGINLMTFDNADELYKVKQHHPNSRLLLRISTDDSNSLCRLSLKFGASLDDTGKLLDIAKSLELNVVGVSFHVGSGSYDPSAFLDAIQRSRQVFDQGLERGFNFDLLDIGGGFMNDSFDGVADLIRSALDTYFDPSIRVISEPGRFFVSSSFTLAVNVIAKRKLDDEEKVMYYVNDGVYGSLNCILFDHQHPVARVLKCGSRFVYNDLVGTGQHRCFIWGPTCDSLDVIANDAHLPYELNVGDWIYFEDAGAYTVAAASCFNGFKTSRIVYLDTDILD
|
Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis.
|
Q9UQW9
|
Q8EUB6
|
RL2_MALP2
|
50S ribosomal protein L2
|
Malacoplasma
|
MPIRRVKARSSGIRQTVIIDYKKVLTTSTPEKSLVVSLKKHSGRNNNGKITVRHHGGGYKKKYRIIDFKRDKINKVATVKSIEYDPNRTSFISLVVYEDGEKRYIIAPKDLKIGDRILSSNKQIDIKVGNALPISLIPEGTFVHNIELYPGRGGQMIRSAGSSAQILGKDETGEYTIVKLSSGEVRKIANGCMATIGVVSNEDHNLVVIGKAGTNRHRGIRPTVRGSAMNPNDHPHGGGEGRSPVGHDAPRTPWGKRHMGVKTRNKKKQSNALIIRRKK
|
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome.
|
Q8EUB6
|
Q9UTN6
|
SNF21_SCHPO
|
RSC complex subunit snf21
|
Schizosaccharomyces
|
MRAEKQYTRNEVEETIVRWKKLKESGATEHDNTEYAQLCDVLRSAQSEIEARRDLKGHIKRCFSSVDKNTEKLILKQQVLAYKKLSQNLPAPDDCILSVLLRLSKDEQLLQSIVKQPLQNSKVDGKVRRDFGSCQITPSAKQQRKYLQYQISEDDAIKNRMFRRMSDLESYPAVMRDVAELKDDNERLNLDTIKRNALVELKKLRLIKQQESLRHQVMHCQPHLRTIVNAVERMSCRRPKLVPQATRLTEVLERQQRSDRERRLKQKQCDYLQTVCAHGREINVRTKNAQARAQKANRAVLAYHSHIEKEEQRRAERNAKQRLQALKENDEEAYLKLIDQAKDTRITHLLRQTDHYLDSLAAAVKVQQSQFGESAYDEDMDRRMNPEDDRKIDYYNVAHNIREVVTEQPSILVGGKLKEYQLRGLQWMISLYNNHLNGILADEMGLGKTIQTISLITHLIEKKRQNGPFLVIVPLSTLTNWTMEFERWAPSIVKIVYKGPPQVRKALHPQVRHSNFQVLLTTYEYIIKDRPLLSRIKWIYMIIDEGHRMKNTQSKLTNTLTTYYSSRYRLILTGTPLQNNLPELWALLNFVLPRIFNSIKSFDEWFNTPFANTGGQDKMELTEEESLLVIRRLHKVLRPFLLRRLKKDVEAELPDKVEKVIRCQMSGLQQKLYYQMKKHGMLYVEDAKRGKTGIKGLQNTVMQLKKICNHPFVFEDVERSIDPTGFNYDMLWRVSGKFELLDRILPKLFRSGHRILMFFQMTQIMNIMEDYLHYRQWRYLRLDGSTKADDRSKLLGVFNDPTAEVNLFLLSTRAGGLGLNLQTADTVIIFDSDWNPHQDLQAQDRAHRIGQTKEVRIYRLITEKSVEENILARAQYKLDIDGKVIQAGKFDNKSTPEEREAFLRSLLENENGEEENDEKGELDDDELNEILARGDDELRLFKQMTEDLERESPYGKNKEKERLIQVSELPEFYQREEPEKTTDLLQEEPLGRGARRRTPVVYDEAVRDAQWMAEMDMESEARPTRGRPKRNIASVDETPALTLNGKPKKKRGPAPDTLTSEHRSLLRRVCLEIYKAVNELEDDNGRPLNKLFLELPSKKLYPDYYMIIKSPIALDAIRKHINGTFYKTLEAMKSDLMTMFNNARTYNEEGSFVYEDANKMQTAMETKIEELEEDGTLATLRGMEAEATSQLEDRIENEA
|
Helicase. Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. Controls particularly membrane and organelle development genes.
|
Q9UTN6
|
Q5PG96
|
HPCH_SALPA
|
4-hydroxy-2-ketoheptane-1,7-dioate aldolase
|
Salmonella
|
MKNAFKDALKAGRPQIGLWLGLANSYSAELLAGAGFDWLLIDGEHAPNNVQTVLTQLQAIAPYPSQPVVRPSWNDPVQIKQLLDVGAQTLLIPMVQNADEARNAVAATRYPPAGIRGVGSALARASRWNRIPDYLHLANDAMCVLVQIETREAMSNLASILDVDGIDGVFIGPADLSADMGFAGNPQHPEVQAAIENAIVQIRAAGKAPGILMANEALAKRYLELGALFVAVGVDTTLLARGAEALAARFGAEKNLSGASGVY
|
Catalyzes the reversible retro-aldol cleavage of 4-hydroxy-2-ketoheptane-1,7-dioate (HKHD) to pyruvate and succinic semialdehyde.
|
Q5PG96
|
A6VJ05
|
MTD_METM7
|
Coenzyme F420-dependent N5,N10-methylenetetrahydromethanopterin dehydrogenase
|
Methanococcus
|
MVVKIGILKCGNIGMSPVVDLCLDERADRNDIDVRVLGSGAKMGPEQVEEVAKKMVEEVKPDFIVYIGPNPAAPGPKKAREILSAGGIPTVIIGDAPGIKDKDAMAEEGLGYVLIKCDPMIGARRQFLDPVEMAMFNADVIRVLAGTGALRVVQNAIDDMVFAVEEGKEIPLPKIVITEQKAVDAMDFANPYAKAKAMAAFVMAEKVADIDVKGCFMTKEMEKYIPIVASAHEAIRYAAKLVDEARELEKATDAVSRKPHAGEGKILNKCKLMAKPE
|
Catalyzes the reversible reduction of methenyl-H(4)MPT(+) to methylene-H(4)MPT.
|
A6VJ05
|
P75330
|
P30_MYCPN
|
Cytadhesin P30
|
Mycoplasma
|
MKLPPRRKLKLFLLAWMLVLFSALIVLATLILVQHNNTELTEVKSELSPLNVVLHAEEDTVQIQGKPITEQAWFIPTVAGCFGFSALAIILGLAIGLPIVKRKEKRLLEEKERQEQLAEQLQRISAQQEEQQALEQQAAAEAHAEAEVEPAPQPVPVPPQPQVQINFGPRTGFPPQPGMAPRPGMPPHPGMAPRPGFPPQPGMAPRPGMPPHPGMAPRPGFPPQPGMAPRPGMPPHPGMAPRPGFPPQPGMAPRPGMQPPRPGMPPQPGFPPKR
|
Adhesin necessary for successful cytadherence and virulence.
|
P75330
|
Q2RAR6
|
CCDA1_ORYSJ
|
Cytochrome b6f biogenesis protein CCDA1
|
Oryza sativa
|
MLCVAMAARPVSSTTSTCRPCLPAQVSASKPSTSSSPGTGVLVGVPRERGSSVSKAAIRGARLEAAARCSLVRQRPMLLATVAVGSLVAAGAANATEIGDSLLGSSGLALADLSVGDWFGNLLYSAGQQANEAVQDQLSALSFTSLAVIFGAGLVTSLSPCTLSVLPLTLGYIGAFGSGKDRSEVVGNSVAFSLGLATTLAILGVAASFAGKAYGQVGQGLPVAASGLAVIMGLNLLEVIELQLPSFFSDYDPRAAAANLPSSVQAYLAGLTFALAASPCSTPVLATLLGYVATSRDPIVGGSLLLTYTTGYVAPLLIAASFAGALQSLLSFRRYSAWINPISGAFLLGGGVYTLLDRLFPATSMVM
|
Probably involved in the transfer of reducing equivalents from stroma to thylakoid lumen and required for the biogenesis of the plastid cytochrome b6f complex.
|
Q2RAR6
|
Q3KLH1
|
RL23_CHLTA
|
50S ribosomal protein L23
|
Chlamydia
|
MKDPYDVVKRHYVTEKAKMLEGLSLGDGEGKKKGSFCKDPKYIFIVAGDATKPMIAEAIEAIYSAKGVKVKKVNTMCVKPQPTRIFRGRRKGRTAGFKKAIVTFVDGHSIG
|
One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome.
|
Q3KLH1
|
A7I3Y5
|
PDXJ_CAMHC
|
Pyridoxine 5'-phosphate synthase
|
Campylobacter
|
MLLGVNIDHIAVLREARQVNDPDILMGMYAAIIGGADQITTHLREDRRHINENDVKDIINHSRVPVNLECSINEEIIDFVCKFRPHRATLVPEKREELTTEGGLNLSTAGLENIINRLKNEGIKVSLFIDTSRENIDIASELAVDCIELHTGTYANIFNMLNSNIALTKYSIKNYEKSREDLQNLLKDELANIKHLAAYAKGLGLKVAAGHGLNYQNVASLTKNSEIFELNIGQSIIARAIFVGMKTAVCEMKELIK
|
Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
|
A7I3Y5
|
P0DPV0
|
TXA1B_SCODE
|
Toxin SSD449
|
Scolopendra
|
MNKLTIIFFTILLLTYIIVEKEALKIEDLPEPESYKKAKQLAVKDANGDKRAEGIALDFLRQNRRNCTVNCDLVLTCPLLTPECCPKKNDDCLKLDTVKNG
|
Voltage-gated calcium channel inhibitor.
|
P0DPV0
|
A9N275
|
ASTB_SALPB
|
N-succinylarginine dihydrolase
|
Salmonella
|
MTAHEVNFDGLVGLTHHYAGLSFGNEASTRHRFQMSNPRLAVKQGLLKMKALADAGFPQAVIPPHERPFIPALRQLGFTGSDEQILDKVARQAPRWLSSVSSASPMWVANAATVCPSADALDGKVHLTVANLNNKFHRALEVPVTEALLRAIFRDESQFSVHSALPQVALLGDEGAANHNRLGGEYGSAGVQLFVYGREEENEIRPARYPARQSREASEAVARLNQVNPQQVIFAQQNPEVIDQGVFHNDVIAVSNRQVLFCHEAAFARQKVLINQLRTRVDGFMAIEVPAGEVSVSDAVATYLFNSQLLSRDDGSMLLVLPRECQDHAGVWRYLNKLVAEDNPISAMQVFDLRESMANGGGPACLRLRVVLTEEERRAVNPAVMMNDALFTALNAWADRYYRDRLTAADLADPLLLREGREALDVLTRLLDLGSVYPFQQTGAADG
|
Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-succinylornithine, ammonia and CO(2).
|
A9N275
|
Q83N58
|
NHAA_TROW8
|
Sodium/proton antiporter NhaA
|
Tropheryma
|
MSIIRSERYSAIFLLCSAALAIIFANVLDPDTWHAVHSAVSEYHIFGLITPHDIVADFLLAVFFFAVAIELKHELVKGELSSFSKAIIPGVCAAGGILVPISIYLSVASVLPNGWPVPTATDVAFSLGILAIFGSSLPSKVRIFLLALAVLDDLAGIVIIATAFSVSISYWWIIVACITVGLFGFCSYRLARCKTSKTFLIIPAMLLCALAAWVSVYQSGIHATIAGVMLGIMLNRKQGAAIEHALEPYINGIILPAFAFLAAMVRVPHLPLDEISPALWGILLGLLFGKLLGISVFGIIALKFFRKKSISFFNLLVVSALGGIGFTVSLLMNELAFLGTPVHEQGVIAVLIGSLLSAILAIILMRCYKGRKSKSLPGRKGRVSH
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Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
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Q83N58
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