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
|
|---|---|---|---|---|---|---|
Q9HEZ1
|
XYNA_PHACH
|
1,4-beta-D-xylan xylanohydrolase A
|
Phanerodontia
|
MKLSASFAALALLLPFVQAQSPVWGQCGGIGWTGPTTCTAGNVCQEYSAYYSQCIPASQATSVTSVSTAPNPPPTSHTSTSSAPSGASTSTAKLNTLAKAKGKLYFGTATDNGELSDTAYTAILDDNTMFGQITPANSMKWDATEPQQGQFTFSGGDQIANLAKSNGMLLRGHNCVWYNQLPSWVSNGKFTAAQLTSIIQNHCSTLVTHYKGQVYAWDVVNEPFNDDGSWRTDVFYNTLGTSYVQIALEAARAADPDAKLYINEYNIEYAGAKATSLLNLVKTLKAASVPLDGIGFQSHFIVGQVPTGLQSQLTTFAAQGVEVAITELDIRMTLPSTPALLAQQKTDYSNVIKACASVEACVGVTVWDWTDKYSWVPNTFSGQGAACPWDQNFVRKPAYDGIAIGFGN
|
Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.
|
Q9HEZ1
|
P18026
|
TBB2_MAIZE
|
Beta-2-tubulin
|
Zea
|
MREILHIQGGQCGNQIGSKFWEVVCDEHGIDPTGRYMGTSDVQLERVNVYYNEASCGRFVPRAVLMDLEPGTMDAVRTGPYGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMMTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRSLTVPELTQQMWDSKNMMCAADPRHGRYLTASAMFRGKMSTKEVDEQMINVQNKNSSYFVEWIPNNVKSSVCDIPPRGLSMSSTFVGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEEADYEEEEAAAE
|
Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
|
P18026
|
A3MZ07
|
UBIG_ACTP2
|
3-demethylubiquinone 3-O-methyltransferase
|
Actinobacillus
|
MNNIDQTELDKFEKMAATWWDPNGSFKPIHLLNPLRLDYIQQKANGLFGKKVLDVGCGGGILSEAMARAGATVTGIDMTTEPLEVARKHAEENGLSIDYRQTTIEDFVQNQTACHAEKFDVITCMEMLEHVPDPLSIIQSCKALLKPDGVLFFSTINRTLKAYMLVIIGAEYVLKMLPKGTHEFEKFIKPAELLNWCDMADLRCQEMKGYHFNPVTEKFWLNNDVSCNYIAMLK
|
O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
|
A3MZ07
|
D5AKX9
|
TAUR_RHOCB
|
HTH-type transcriptional regulator TauR
|
Rhodobacter
|
MAIPVESFFLAPGGQGSLQHRLRQMVTEGILSGRFRPGDRMPSTRALAAHLGVARITVTLAYADLVASDYLLARGRSGTFVSAAAPDARKARPLPRDGARTDWARLLHPRAQGLPRPDRPRDWSLYRYPFIYGQADPELFDHQNWRACALQALGRREFHRLSADCYDEDDPLLVEYILRHILPRRGIAAVPSEVLITMGAQNGLWLAAQVLLGPGERAAMENPGYPGTRAVLGTTGAEVLSVDVDDRGLVPAQLPARLKLVVTTASHHCPTNATLPVERRLALLAAAEAGDFLILEDDYEFEMSFLQSAAPSLKSLDAGGRVVHVGSFSKSLFPGLRLGYLVAPAPFVAAVRALRATVLRHPPGQLQRTLALFLSLGHYDALVARMKAAYRLRREVMTKAIEDNGLQIAGQGGFGGSSFWMQAPGAVDTEDLALRLRAEGVLIEPGRVFFDPARERRNFYRLAYSSIGPAAIPEGIARIARALR
|
Transcriptional activator, which is essential for taurine-dependent expression of the tpa-tauR-xsc operon. Acts by binding to direct repeats in the promoter region.
|
D5AKX9
|
Q8EHI9
|
TORA_SHEON
|
Trimethylamine-N-oxide reductase
|
Shewanella
|
MNRRDFLKGLASTSFVALGGSSVLAPLNALANTGLNENEWLTTGSHFGAFKIKRKNGMIAEVKAFDLDKYPTDMINGIRGMVYNPSRVRYPMVRLDFLLKGHKSNTQQRGDFRFVRVTWDKALKLFKHSLDEVQTKYGPSGLHAGQTGWRATGQLHSSTSHMQRAVGMHGNFVKKIGDYSTGAGQTILPYVLGSTEVYAQGTSWPLILENSNTIVLWSNDPYKNLQVGWNAETHEAFAYLAQLKEKVKQGKIRVISIDPVVTKTQAYLGCEQLYVNPQTDVTLMLAIAHEMITQKLHDEKFIQGYSLGFEEFVPYVMGTKDGIAKTPEWAAPICGVEPHIIRDLAKTLVKGRTQIMMGWCIQRQQHGEQPYWMAAVLATMIGQIGLPGGGISYGHHYSSIGVPATTAAAPGAFPRNLDENQKPLFDSTDFKGASSTIPVARWIDAILEPGKTIDANGSKVVYPDIKMMIFSGNNPWNHHQDRNRMKQAFQKLECVVSIDVNWTATCRFSDIVLPACTTYERNDIDVYGAYANRGILAMQKMVEPLFESLSDFEIFTRFAALLGKEKEYTRNMSEMEWIETLYNECKAANAGKYEMPDFATFWKQGYVHFGEGELWTRHADFRNDPEINPLGTPSGLIEIFSRKIEQFGYDDCQGHPMWMEKAERSHGGPGSNKYPMWLQSCHPDHRLHSQMCESKEYRETYTVNGREPVYISPEDAKTRGIKDGDIVRVFNDRGQLLAGAVVSDRFPKGVVRIHEGAWYGPVGKDGSVEGGAEIGALCSYGDPNTLTLDIGTSKLAQACSAYTCLVEFEKYQGKAPKVSSFDGPIEVEI
|
Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an anaerobic reaction coupled to energy-yielding reactions.
|
Q8EHI9
|
Q82ZW3
|
THII_ENTFA
|
tRNA 4-thiouridine synthase
|
Enterococcus
|
MKYTEIMVRYGELSTKGKNRKTFIMQLAQNVKRALADFPALKIHADRDRMHILLNGEDSEEVIPKLSKVFGIQNFSPSIRIEKEMPAIRAMVQEVVREVYTPGKTFKITAKRSDHSFELDSNGLNQELGGAVIEAIPEIQVQMKKPDINLRIEIRKDAAYLSYETIRGAGGLPVGTSGRGMLMLSGGIDSPVAGYLAMKRGVEVEAVHFASPPYTSEQALQKAKDLAEKLVPYVGTIQFIEVPFTEIQEEIKRVVPQGYLMTITRRLMLRLTDAIREMRKGLVIINGESLAQVASQTLQSMVAINEVTSTPIIRPVVSMDKTEIIEIAEKIDTFELAIQPFEDCCTIFAPPQPKTRPRLDKAQEYEARLDLEGLMARALEGLKITEISAETAKDKQEDEFADFL
|
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.
|
Q82ZW3
|
Q6R3L0
|
YSL1_ARATH
|
Protein YELLOW STRIPE LIKE 1
|
Arabidopsis
|
MEIEQRRIMKREGEEEEDNNQLSLQEEEPDTEEEMSGRTIEPWTKQITVRGVFVSIVIGVVFSVIAQKLNLTTGIVPNLNSSAALLAFVFVQTWTKILKKSGFVAKPFTRQENTMIQTSAVACYGIAVGGGFASYLLGLNHKTYVLSGVNLEGNSPKSVKEPGLGWMTAYLFVVCFIGLFVLIPLRKVMIVDLKLTYPSGLATAVLINGFHTQGDAQAKKQVRGFMKYFSFSFLWGFFQWFFSGIEDCGFAQFPTFGLKAWKQTFFFDFSMTFVGAGMICSHLVNLSLLLGAILSYGLMWPLLDKLKGSWFPDNLDEHNMKSIYGYKVFLSVALILGDGLYTFVKILFVTIANVNARLKNKPNDLDDVGHKKQRKDLKEDENFLRDKIPMWFAVSGYLTFAAVSTVVVPLIFPQLKWYYVIVAYIFAPSLAFCNAYGAGLTDINMAYNYGKIGLFVIAAVTGRENGVVAGLAGCGLIKSVVSVSCILMQDFKTAHYTMTSPKAMFASQMIGTVVGCIVTPLSFFLFYKAFDIGNPNGEFKAPYALIYRNMAILGVQGFSALPLHCLQMCYGFFGFAVLVNVVRDLTPAKIGRFMPLPTAMAVPFLVGAYFAIDMCVGTLIVFVWEKMNRKKAEFMVPAVASGLICGEGLWTLPAAVLALAGVKPPICMKFLAS
|
Involved in iron loading of the seeds. Acts probably as a transporter of iron- and metal-nicotianamine chelates.
|
Q6R3L0
|
Q53M52
|
TBA2_ORYSJ
|
Tubulin alpha-2 chain
|
Oryza sativa
|
MRECISIHIGQAGIQVGNACWELYCLEHGIQPDGQMPGDKTVGGGDDAFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGDYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTVYPSPQVSTSVVEPYNSVLSTHSLLEHTDVAVLLDNEAIYDICRRSLDIERPTYTNLNRLVSQVISSLTASLRFDGALNVDVNEFQTNLVPYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAFEPSSMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKRTIQFVDWCPTGFKCGINYQPPSVVPGGDLAKVQRAVCMISNSTSVVEVFSRIDIKFDLMYSKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGSEFDDGDEGDEGDEY
|
Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
|
Q53M52
|
E5KCJ8
|
Y3IP1_TOBAC
|
Ycf3-interacting protein 1, chloroplastic
|
Nicotiana
|
MASNMLQLSLPPLSSSSSSLPFLSSSVYVLPFTHQRRHFSFFNVQNYRFRLSRSTSLGPLFVNKEEDSATYAVTEEEEDNDDDDPDPQSLEYVSQIKRVLELLKRNRDMLFGEVKLTIMIEDPRDVERRRLLGIDDENAPTRDDLAAALEEINEGKVPKDFAALQMLAEEMNSWPNLEVEATKQNKPGRSLYAKATDTGIDPKEAAKRLKIDWDSAAEIDESAESDEPDVPPALGYGALYLVSAFPIIIGISVVLILFYNSLQ
|
Nuclear genome-encoded factor that participates in photosystem I (PSI) biogenesis. Cooperates with the plastid genome-encoded protein PSI assembly Ycf3 in the assembly of stable PSI units in the thylakoid membrane.
|
E5KCJ8
|
Q9LSZ3
|
VUP1_ARATH
|
Vascular-related unknown protein 1
|
Arabidopsis
|
MMDTFSCNSYEQNHPHDDDIDIDAHDHDSHGGDHQEESGWTTYLDDFSNQYRTTHHEENDHQDKSSYSLLATSTSLVSDAATHAFSGKSFPVNFPAKLKFGRGRTKKICEDDSLEDTASSPVNSPKVSHFEHIQTPPRKIEDYVSSSFVMGNIRGMGDHQIQIQEGGEQKVTLMRNLIDGNNNNNNNNMDLRSRGLCVVPISMLANFNGRC
|
Involved in the regulation of xylem development and growth. May regulate secondary wall formation during vascular development by modulation of brassinosteroid, gibberellin and auxin hormone signaling pathways.
|
Q9LSZ3
|
Q2KA54
|
UVRC_RHIEC
|
Excinuclease ABC subunit C
|
Rhizobium
|
MNGRKLPDGGVLYDDTDESEDEIEVEGDVSAAPLAVAVDWNAGSLNETGLVGAELIGEFVKRLPNSPGVYRMLNAEGDVLYVGKARSLKKRVGNYAVGRVHSNRIAQMVRQTANMEFVTTRTETEALLLEANLIKRLRPRFNVLLRDDKSFPYILITGDHRAPAIFKHRGARARKGDYFGPFASAGAVGRTINSLQRAFLIRTCTDSVFETRTRPCLLYQIKRCSGPCTHEVSDEGYAELVQEAKDFLSGKSQKVKSHMAEAMNQAAEDLDFERAAIYRDRLAALSHVQSHQGINPAGVDEADVFAIHHEGGVSCIQVFFFRTGQNWGNRAYFPKADPQLSSAEVLNAFLAQFYDDKPVPKQIMLSETAEELELLAAALSEKAGHKVSILVPRRGEKRDLVDHVVGNAREAHGRKLAETASQSRLLEGFKETFGLAYAPQRIEIYDNSHIMGTNAVGGMVVAGPEGFVKNQYRKFNIKSTDITPGDDFGMMKEVMTRRFSRLIKEEGIPDRTAQAAAADAADMPFPAWPDVILIDGGQGQMTAVRAILAELGITDSVTAIGIAKGVDRDAGRERFFAPGRESFTLPPRDPVLYFIQRMRDEAHRFAIGSHRVRRKKEMVKNPLDEIGGIGPSRKRALLQHFGTAKAVSRAALSDLMAVEGISEAVAKQVYNHFHEDAAK
|
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
|
Q2KA54
|
B2SDJ2
|
TDH_FRATM
|
L-threonine 3-dehydrogenase
|
Francisella
|
MKALAKLKKQPGIWIINDAPIPEYGYNDVLIKIKKTAICGTDLHIYNWDKWSQNTIPVPMITGHEFAGEVVAKGDGVTSVDIGDRVSGEGHLVCGQCRNCRAGKRHLCRKTIGIGVNVQGAFAEYLVMPAVNVFKIPDSISDDIASTFDPMGNAIHTALSFNLTGEDVLITGAGPIGLMVVKIARFCGARRIVITDINEYRLQMARDFGATVALNVAPFKNQDELVKQMRKVMSDIGMTEGFDVGLEMSGINSAISMMLDVMNHGGKLSLLGISAGDISVDWGAILFKGLTLKGIYGREMFETWYLMTSMLQAGMDMNPIITHRLHIDEFQKGFEIMKSGQCGKVILDWSS
|
Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate.
|
B2SDJ2
|
A9CES6
|
TAGPE_AGRFC
|
D-tagatose 6-phosphate 4-epimerase
|
Agrobacterium tumefaciens complex
|
MTAILENLAAARRAGKPAGITSVCSAHPVVLRAAIRRAAASQTAVLIEATCNQVNHLGGYTGMTPRDFVAFVNSIAAEEGLPAELLIFGGDHLGPNPWRREKAEDALTKAAAMVDAYVTAGFRKIHLDASMGCAGEPAALDDVTIAHRAAKLTAVAEKAATEAGLPKPLYILGTEVPVPGGADHVLETVAPTEPQAARNTIDLHREIFAQHGLSDAFERVIAFVVQPGVEFGSDNVVAYDPQAAQSLSAVLDGEPRLVFEAHSTDYQTEPALAALVRDGYPILKVGPGLTFAYREALYALDMIASEMVGTYGDRPLARTMEKLMLSAPGDWQGHYHGDDITLRLQRHYSYSDRIRYYWTRPEALAAVSTLHKALDGKTIPETLLRQYLGELPLAAVAGKEPEEVLVAAVDQVLATYHAATGEGRH
|
Involved in galactitol and D-altritol catabolism. Catalyzes the epimerization of D-tagatose 6-phosphate to D-fructose 6-phosphate.
|
A9CES6
|
P55916
|
UCP3_HUMAN
|
Solute carrier family 25 member 9
|
Homo
|
MVGLKPSDVPPTMAVKFLGAGTAACFADLVTFPLDTAKVRLQIQGENQAVQTARLVQYRGVLGTILTMVRTEGPCSPYNGLVAGLQRQMSFASIRIGLYDSVKQVYTPKGADNSSLTTRILAGCTTGAMAVTCAQPTDVVKVRFQASIHLGPSRSDRKYSGTMDAYRTIAREEGVRGLWKGTLPNIMRNAIVNCAEVVTYDILKEKLLDYHLLTDNFPCHFVSAFGAGFCATVVASPVDVVKTRYMNSPPGQYFSPLDCMIKMVAQEGPTAFYKGFTPSFLRLGSWNVVMFVTYEQLKRALMKVQMLRESPF
|
UCP are mitochondrial transporter proteins that create proton leaks across the inner mitochondrial membrane, thus uncoupling oxidative phosphorylation. As a result, energy is dissipated in the form of heat. May play a role in the modulation of tissue respiratory control. Participates in thermogenesis and energy balance.
|
P55916
|
B5Z672
|
UREE_HELPG
|
Urease accessory protein UreE
|
Helicobacter
|
MIIERLVGNLRDLNPLDFSVDYVDLEWFETRKKIARFKTRQGKDIAIRLKDAPKLGLSQGDILFKEEKEIIAVNILDSEVIHIQAKSVAEVAKICYEIGNRHAALYYGESQFEFKTPFEKPTLALLEKLGVQNRVLSSKLDSKERLTVSMPHSEPNFKVSLASDFKVVMK
|
Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly.
|
B5Z672
|
Q9V074
|
TYW31_PYRAB
|
tRNA wyosine derivatives biosynthesis protein Taw3 1
|
Pyrococcus
|
MRFTENFERAKKEALISLEIALRRGEVDEDIIPLLKKINEKPNYFTTSSCSGRISIMEMPDFGDKVNAKWLGKWHREVSLDEVLEAIRKHREGQLWLLVRSPILHVGARTLEDGIKLLNLGVSCGFKYSNIKSISDRKLIVEIRSTERLDALLGENGEILVSDDYMRKLVEIANAQVRRFKRKLKRFEERIEEL
|
S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wyosine derivatives biosynthesis pathway. Probably methylates N-4 position of wybutosine-86 to produce wybutosine-72.
|
Q9V074
|
A3QGU3
|
TRUB_SHELP
|
tRNA-uridine isomerase
|
Shewanella
|
MARKPRGRLVDGIVLLDKDTGMSSNFALQRVKRIYNAAKAGHTGALDPLATGMLPICLGEATKFSQHLLDADKRYLVTAKLGVRTDTSDSDGEVVQTRPINFTEQQLEEALEHFRGETMQVPSMYSALKYQGQPLYKYAREGKEVPREARPIKVFELNFIKLEGDELTLDIHCSKGTYIRTITDDLGEMLGCGAHVIMLRRTGVAGYPYDKMVTLEQLEALLAKAQEEERPPKELLDPLLLPMDTAVSGLKEINVSDELAHYLMNGNPVQVANLPIDELVRITLGEAKQFVGIGQMNDDGLLAPKRLVVLHDEQA
|
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
|
A3QGU3
|
Q940K0
|
UNI_ARATH
|
Protein UNI
|
Arabidopsis
|
MGSCFSLQVSDQTLNRIFNCLIGKSYIRTLEKNLRALQREMEDLRAIQHEVQNKVARDEARHQRRLEAVQVWLDRVNSVDIECKDLLSVTPVELQKLCLCGLCSKYVCSSYKYGKKVFLLLEEVKKLNSEGNFDEVSQPPPRSEVEERPTQPTIGQEDMLEKAWNRLMEDGVGIMGLHGMGGVGKTTLFKKIHNKFAEIGGTFDIVIWIVVSKGVMISKLQEDIAEKLHLCDDLWKNKNESDKATDIHRVLKGKRFVLMLDDIWEKVDLEAIGIPYPSEVNKCKVAFTTRSREVCGEMGDHKPMQVNCLEPEDAWELFKNKVGDNTLSSDPVIVELAREVAQKCRGLPLALNVIGETMSSKTMVQEWEHAIHVFNTSAAEFSDMQNKILPILKYSYDSLGDEHIKSCFLYCALFPEDGEIYNEKLIDYWICEGFIGEDQVIKRARNKGYAMLGTLTRANLLTKVGTYYCVMHDVVREMALWIASDFGKQKENFVVQAGVGLHEIPKVKDWGAVRKMSLMDNDIEEITCESKCSELTTLFLQSNKLKNLPGAFIRYMQKLVVLDLSYNRDFNKLPEQISGLVSLQFLDLSNTSIEHMPIGLKELKKLTFLDLTYTDRLCSISGISRLLSLRLLRLLGSKVHGDASVLKELQQLQNLQELAITVSAELISLDQRLAKLISNLCIEGFLQKPFDLSFLASMENLSSLRVENSYFSEIKCRESETESSYLRINPKIPCFTNLSRLEIMKCHSMKDLTWILFAPNLVVLLIEDSREVGEIINKEKATNLTSITPFLKLEWLILYNLPKLESIYWSPLPFPVLLTMDVSNCPKLRKLPLNATSVSKVEEFEIHMYPPPEQENELEWEDDDTKNRFLPSIKPYKYFVYPGMSFLTV
|
Involved in disease resistance via the salicylic acid (SA) signaling pathway . Involved in shoot architecture development via the cytokinin signaling pathway .
|
Q940K0
|
A7MLI3
|
ZNTB_CROS8
|
Zinc transport protein ZntB
|
Cronobacter
|
MEAIKGSEVNVPDAVIAWLLDGHGGVKPLQDDAVIDKDHPCWLHLNYANPESAQWLTETPLLPNLVRDALAGESLRPRVTRMGDGTLITLRCINGSTDERPDQLVAMRLYIDERLIVSTRQRKVLALDDIIHDLNEGSGPADVGGWLVDACDALTDHASEFIEELHDKIIDLEDNLLEEIVPPRGVLALLRKQLIVMRRYMSPQRDVFSRLASERFSWMTDDHRRRMQDIADRLGRGLDEIDACIARTAVMADEISQTMQESLSRRSYTMSLMAMVFLPSTFLTGLFGVNLGGIPGGGWHLGFSVFCVALVLLIGGVTWWLHRSKWL
|
Zinc transporter. Acts as a Zn(2+):proton symporter, which likely mediates zinc ion uptake.
|
A7MLI3
|
Q8UEP9
|
TATA_AGRFC
|
Sec-independent protein translocase protein TatA
|
Agrobacterium tumefaciens complex
|
MGSFSVWHWLIVLVIVLVLFGRGKIPELMGDVAKGIKSFKKGMADEDQTPPPADANANAKTVDHKADEIK
|
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.
|
Q8UEP9
|
Q8WZE0
|
TBB_USTVI
|
Beta-tubulin
|
Microbotryum
|
MREIVSLQAGQCGNQIGTKFWEVVSEEHGIDGTGQYTGTSDLQLERINVYYNETGTGKYVPRAVLVDLKPGTMDVIQGGPLGGLFRPDNFVFGQSGAGNNWAKGHYTEGAELVDQVLDVVRKEAEGTDCLQGFQLTHSLGGGTGSGMGTLLVSKIREEFPDRMMATFSVVPSPKVSDTVVEPYNAVLSVHQLVENSDETFCIDNEALYDICFRTLKLSAPTHGDLNGLVSIVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRLHFFTVGFAPLTARGSSQYRAVTVAELTAQMFDAKNMMAASDPRHGRYLTVAAYFRGKVSMKEVEDQMVSIQQKNSQYFVEWIPNNVQSAHCEVAPRGLKMSVTFIGNNTSIQELFKRVGDHFDVMFRRRAFLHWYTGEGMDEMEFSEASANMHDLIAEYTQYQEAGVDDEEEVAYEEEPQE
|
Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
|
Q8WZE0
|
A0KEH3
|
UBID_AERHH
|
Polyprenyl p-hydroxybenzoate decarboxylase
|
Aeromonas
|
MKYKDLRDFIAQLEQSGQLKRISREIDPYLEMTEISDRTLRAGGPALLFENPKGYTMPVLTNLFGTPDRVAMGMGQPNVAALRQVGIWLSYLKEPEPPRGFKELMEKLPIFKQVLNMPTKRLSSAPCQQRVLEGEAVDLDQIPIQHCWPGDVAPLVTWGLTITRGPYKKRQNLGIYRQQKIGKNKLIMRWLDHRGGAIDFREWQEAHPGERFPVVVALGADPATILGAVTPVPDTLSEYAFAGLLRGSRTEVVKAVSCDLEVPASAEIVLEGYLEPGEMAPEGPYGDHTGYYNEVDEFPVFTITHMTMRKDAIYHSTYTGRPPDEPAVLGVALNEVFVPLLQKQFPEIVDFYLPPEGCSYRMAVVTIKKRYPGHAKRVMLGVWSFLRQFMYTKFVIVCDDDINARDWKDVIWAITTRMDPARDTTLIEHTPIDYLDFASPVSGLGSKMGLDATNKWPGETNREWGQPIVQDEAVKQKIDALWDELNILG
|
Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis.
|
A0KEH3
|
A1YG60
|
ZKSC8_PANPA
|
Zinc finger protein 192
|
Pan
|
MAEESRKPSAPSPPDQTPEEDLVIVKVEEDHGWDQESSLHENNPLGQEVFRLRFRQLCYQETLGPREALIQLRALCHQWLRPDLNTKEQILELLVLEQFLTILPEELQTLVKEHQLENGEEVVTLLEDLERQIDILGRPVSARVHGHRVLWEEVVHSASAPEPPNTQLQSEATQHKSPVPQESQERSMSTSQSPTRSQKGSSGDQEMTATLLTAGFQTLEKIEDMAVSLIREEWLLDPSQKDLSRDNRPEDFRNVFSLGGETRSENRELASKQVISTGIHPHGETAAKCNGDVIRGLEHEEARDLLGRLERQRGNPTQERRHKCDECGKSFAQSSGLVRHWRIHTGEKPYQCNVCGKAFSYRSALLSHQDIHNKVKRYHCKECGKAFSQNTGLILHQRIHTGEKPYQCNQCGKAFSQSAGLILHQRIHSGERPYECNECGKAFSHSSHLIGHQRIHTGEKPYECDECGKTFRRSSHLIGHQRSHTGEKPYKCNECGRAFSQKSGLIEHQRIHTGERPYKCKECGKAFNGNTGLIQHLRIHTGEKPYQCNECGKAFIQRSSLIRHQRIHSGEKSESISV
|
May be involved in transcriptional regulation.
|
A1YG60
|
B2HLS6
|
Y358_MYCMM
|
Putative S-adenosyl-L-methionine-dependent methyltransferase MMAR_0358
|
Mycobacterium
|
MPRTADDSWDIATSVGATAVMVALARAAETASETPLIRDQFAEPLVSTPELAAVREQVAAWWAQTDDDDDPDFTVDSQQMTDYLAVRTHFFDSYFIDAVAAGIRQVVILAAGLDSRAYRLDWPGGTTVYEIDLPKVLDYKEHTLARHGAAPVAALRAVPVDLRHDWPQALRDAGFQTSLPTAWLAEGLLPFLPAAAQHALFTAIDANSATGSRVAVEMFGVDEDARRAAEERAQRWARQRAKRQARGQDTSFDPFDLWFDDEGQPDPADWFAAHGWTTDSVQAGAEALRLGRTAHSQEGPFVNRFVTAGKP
|
Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity.
|
B2HLS6
|
Q3Y8M6
|
TPM_PENAT
|
Tropomyosin Pen a 1
|
Penaeus
|
MDAIKKKMQAMKLEKDNAMDRADTLEQQNKEANNRAEKSEEEVHNLQKRMQQLENDLDQVQESLLKANIQLVEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLTNKLKAAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQTFSELSGY
|
Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction.
|
Q3Y8M6
|
Q8TCW7
|
ZPLD1_HUMAN
|
Zona pellucida-like domain-containing protein 1, secreted form
|
Homo
|
MEQIWLLLLLTIRVLPGSAQFNGYNCDANLHSRFPAERDISVYCGVQAITMKINFCTVLFSGYSETDLALNGRHGDSHCRGFINNNTFPAVVIFIINLSTLEGCGNNLVVSTIPGVSAYGNATSVQVGNISGYIDTPDPPTIISYLPGLLYKFSCSYPLEYLVNNTQLASSSAAISVRENNGTFVSTLNLLLYNDSTYNQQLIIPSIGLPLKTKVFAAVQATNLDGRWNVLMDYCYTTPSGNPNDDIRYDLFLSCDKDPQTTVIENGRSQRGRFSFEVFRFVKHKNQKMSTVFLHCVTKLCRADDCPFLMPICSHRERRDAGRRTTWSPQSSSGSAVLSAGPIITRSDETPTNNSQLGSPSMPPFQLNAITSALISGMVILGVTSFSLLLCSLALLHRKGPTSLVLNGIRNPVFD
|
Glycoprotein which is a component of the gelatinous extracellular matrix in the cupulae of the vestibular organ.
|
Q8TCW7
|
Q8TXJ5
|
TRPD_METKA
|
Anthranilate phosphoribosyltransferase
|
Methanopyrus
|
MSVLERIIRGSDLDREEARDLMCRIVGGELSDVEVAGILVALRCKGYTSEELVGFVDGMMEHAVKVDPDVERLVDTAGTGGDELDTFNASTLAGLTAAAAGVPVAKHGNRSVTSECGSADILEALGVNIEADPDTVKRCIEEVGFGFMFAPKFHPAMKNVMPVRRKLGIRTVFNVLGPLTNPARERVTGQVIGVYSENLLDLVAGALAELGVRRGLVVYGLDGVDELSVTCENEVVYVDDGEVTDRDTVAPEDVGLDRADPKDVAGADPETSAEEARKILGGELPVDHPKVQMTAFNAGAALYVGEAVDSLEKGIQRALDVLEEGRALEVLEKVVDLSS
|
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
|
Q8TXJ5
|
Q9PL12
|
TRMD_CHLMU
|
tRNA [GM37] methyltransferase
|
Chlamydia
|
MEIDILSLFPDYFTSPLQATILGRAIKQGALSIRSRDIREFGLGKWKQVDDAPYSGEGMLLMAEPVVQAIRSVKREKSKVVYLSPQGQLLSAKKSRELSLCPHLILLCGHYEGIDERALASEVDEEISIGDYVLTNGCAAALVLVDALARFIPGVLGNQESAECDSLENGLLEGPHYTRPRVFEGVQVPEILFCGDHQRIANWRKKVSLERTRERRPDLYLQYFYGDRAFWGAQEDPLKMRETSPQAFSVVLEVKDLRKAKKFYSRMFGKEHWDGDKLLLGEKTSLYLQQTNERRGATKVFVELETEDGFVRFLRRWEMLGGQLGEVGMGNLPLRQVFDLDGHIWVVSCVQK
|
Specifically methylates guanosine-37 in various tRNAs.
|
Q9PL12
|
Q95K52
|
ZN283_MACFA
|
Zinc finger protein 283
|
Macaca
|
MGSLRHAWFNTSFSFPSSGFSGFCASPIEESHGALISSCNSRTMTDGLVTFRDVAIDFSQEEWECLDPAQRDLYVDVMLENYSNLVSLDLESTTYETKKIFSEKDIFEINFSQWEMKEKSKTLGLEASIFRNNWKCKSIFKGLKGCQEGYFSQMIISYEEIPSYRKSKSLTPHQSIHNTEKPYVYKERVNACSHGSKLVQHKRTHTAEKHFECKECGKNYLSAYQLNVHQRFHTGEKPYECKECGKTFSWGSSLVKHERIHTGEKPYECKECGKAFSRGYHLTQHQKIHIGVKSYKCKECGKAFFWGSSLAKHEIIHTGEKPYQCKECGKAFSRGYQLTQHQKIHTGKKPYECKICGKAFCWGYQLTRHQIFHTGEKPYECKECGKAFNCGSSLIQHARIHTGEKPYECKECGKAFSRGYHLSQHQKIHTGEKPFECKECGKAFSWGSSLVKHERVHTGEKSHECKECGKNFCSGYQLTRHQVFHTGEKPYECKECGKAFNCGSSLVQHERIHTGEKPYECKECGKAFSRGYHLTQHQKIHTGEKPFKCKECGKAFSWGSSLIKHERVHTNEKTYGCKDCGKAFGSGYQLSVHQRFHTGEKLYQCKEFGKTFTHGSKLVHERTCNDKPYKYKECGEAFLWTTYSNEKIDTDETL
|
May be involved in transcriptional regulation.
|
Q95K52
|
P53781
|
TTP_BOVIN
|
Zinc finger protein 36
|
Bos
|
MDLAAIYKSLLSLSPELPSDLGETESSTSWASSGPWSLSSSDSSLPEVAARLPGRSTSLVEGRSCGWVPPPPGFAPLAPRPSSDWSPSPTSPTATPTTSSRYKTELCRTFSESGRCRYGAKCQFAHGLGELRQASRHPKYKTELCHKFYLQGRCPYGSRCHFIHNPSEDLAAPGHPHVLRQSISFSGLPSGRRTSPPPASLAGPSVSSWSFSPSSSPPPPPGDLLLSPSAFSAAPGHLCRRDPTPACCPSCRRATPNSVWGPVGGLARSPSAHSLGSDPDEYASSGTSLGGSDSPVFEAGVFGPPQPPAAPRRLPIFNRISVSE
|
Zinc-finger RNA-binding protein that destabilizes numerous cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis. Acts as an 3'-untranslated region (UTR) ARE mRNA-binding adapter protein to communicate signaling events to the mRNA decay machinery. Recruits deadenylase CNOT7 (and probably the CCR4-NOT complex) via association with CNOT1, and hence promotes ARE-mediated mRNA deadenylation. Functions also by recruiting components of the cytoplasmic RNA decay machinery to the bound ARE-containing mRNAs. Self regulates by destabilizing its own mRNA. Binds to 3'-UTR ARE of numerous mRNAs. Binds also to ARE of its own mRNA. Plays a role in anti-inflammatory responses; suppresses tumor necrosis factor (TNF)-alpha production by stimulating ARE-mediated TNF-alpha mRNA decay and several other inflammatory ARE-containing mRNAs in interferon (IFN)- and/or lipopolysaccharide (LPS)-induced macrophages. Also plays a role in the regulation of dendritic cell maturation at the post-transcriptional level, and hence operates as part of a negative feedback loop to limit the inflammatory response. Promotes ARE-mediated mRNA decay of hypoxia-inducible factor HIF1A mRNA during the response of endothelial cells to hypoxia. Positively regulates early adipogenesis of preadipocytes by promoting ARE-mediated mRNA decay of immediate early genes (IEGs). Negatively regulates hematopoietic/erythroid cell differentiation by promoting ARE-mediated mRNA decay of the transcription factor STAT5B mRNA. Plays a role in maintaining skeletal muscle satellite cell quiescence by promoting ARE-mediated mRNA decay of the myogenic determination factor MYOD1 mRNA. Associates also with and regulates the expression of non-ARE-containing target mRNAs at the post-transcriptional level, such as MHC class I mRNAs. Participates in association with argonaute RISC catalytic components in the ARE-mediated mRNA decay mechanism; assists microRNA (miRNA) targeting ARE-containing mRNAs. May also play a role in the regulation of cytoplasmic mRNA decapping; enhances decapping of ARE-containing RNAs, in vitro. Involved in the delivery of target ARE-mRNAs to processing bodies (PBs). In addition to its cytosolic mRNA-decay function, affects nuclear pre-mRNA processing. Negatively regulates nuclear poly(A)-binding protein PABPN1-stimulated polyadenylation activity on ARE-containing pre-mRNA during LPS-stimulated macrophages. Also involved in the regulation of stress granule (SG) and P-body (PB) formation and fusion. Plays a role in the regulation of keratinocyte proliferation, differentiation and apoptosis. Plays a role as a tumor suppressor by inhibiting cell proliferation in breast cancer cells.
|
P53781
|
P42660
|
VCP_AEDAE
|
Vitellogenic carboxypeptidase
|
Stegomyia
|
MVKFHLLVLIAFTCYTCSDATLWNPYKKLMRGSASPRRPGESGEPLFLTPLLQDGKIEEARNKARVNHPMLSSVESYSGFMTVDAKHNSNLFFWYVPAKNNREQAPILVWLQGGPGASSLFGMFEENGPFHIHRNKSVKQREYSWHQNHHMIYIDNPVGTGFSFTDSDEGYSTNEEHVGENLMKFIQQFFVLFPNLLKHPFYISGESYGGKFVPAFGYAIHNSQSQPKINLQGLAIGDGYTDPLNQLNYGEYLYELGLIDLNGRKKFDEDTAAAIACAERKDMKCANRLIQGLFDGLDGQESYFKKVTGFSSYYNFIKGDEESKQDSVLMEFLSNPEVRKGIHVGELPFHDSDGHNKVAEMLSEDTLDTVAPWVSKLLSHYRVLFYNGQLDIICAYPMTVDFLMKMPFDGDSEYKRANREIYRVDGEIAGYKKRAGRLQEVLIRNAGHMVPRDQPKWAFDMITSFTHKNYL
|
May play a role in activating hydrolytic enzymes that are involved in the degradation of yolk proteins in developing embryos or may function as an exopeptidase in the degradation of vitellogenin.
|
P42660
|
A0RYD1
|
TRM56_CENSY
|
tRNA ribose 2'-O-methyltransferase aTrm56
|
Cenarchaeum
|
MRIEVLRIGQRAVRDDRVTTHAALVARAFGAERIFMEEVNPQVRDTLADVSSTWGGGFEVELIDSWRALLRSKKGSASIVHLTMYGETIDAAIGSLRRKEKILAVVGAGKVPRDVYELADYNVSIGGQPHSEISALAVFLDRLQEGRQLSKGYGDARRKVLPMRRGKHVLEGEPE
|
Specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs.
|
A0RYD1
|
Q794W0
|
YYCH_BACSU
|
Two-component system WalR/WalK regulatory protein YycH
|
Bacillus
|
MKRENIKTILLTVLVVISLVFTWGIWTFQPNFSEGSSSTESTVRVKHKIEKTTQKLSETVRPRDMFIHDDGAHYKVDDNALYEEIWSDLPHWDVKGIKDISDQYDKAGFKSWFYGIGGSEAKLDLQFSDTIPIDIFQTLFKWSNQSFEYSSFDHILIPFNETKANKKIYLVSYSKQLILEVTVESANYRNIMNDLKNRQSNMPAFSLFSIGSKKEFLLPNKPLTMDKKEFVTESIKTNTFKQALFSDPSIVREDSNYNNRNVLTDGISRLDVNLSQRQVQFQQRNLVQSTSYQTGELIKKSQKYLEDTGSWTDHYQFFNINDSQQLSFYIFMDQIPVINSTAKPFGATSAITVQWANDDILSYKRPNYSLGTNPIKTSETELMGGSEVKMLLSKQTAYDTDKIDQIFLAYQLVSTSTNDDPLVELEPVWAMKVNGKIVPITKDLLRKEGANSGVE
|
Together with YycI, regulates the activity of the two-component system WalR/WalK.
|
Q794W0
|
P85505
|
TXHM1_HERML
|
Neurotoxin Hm-1
|
Heriaeus
|
GCIPYGKTCEFWSGPWCCAGKCKLNVWSMTLSCTRNF
|
Blocks the Nav1.2/SCN2A, Nav1.4/SCN4A, and Nav1.6/SCN8A sodium channels. Reduces the peak amplitude of the sodium current and negatively shifts the steady-state inactivation process. Does not shift the threshold potential of activation or the voltage corresponding to maximal current. Does not change the reversal potential of the sodium current. May act on site 1 of the receptor.
|
P85505
|
Q9P2J2
|
TUTLA_HUMAN
|
Immunoglobulin superfamily member 9A
|
Homo
|
MVWCLGLAVLSLVISQGADGRGKPEVVSVVGRAGESVVLGCDLLPPAGRPPLHVIEWLRFGFLLPIFIQFGLYSPRIDPDYVGRVRLQKGASLQIEGLRVEDQGWYECRVFFLDQHIPEDDFANGSWVHLTVNSPPQFQETPPAVLEVQELEPVTLRCVARGSPLPHVTWKLRGKDLGQGQGQVQVQNGTLRIRRVERGSSGVYTCQASSTEGSATHATQLLVLGPPVIVVPPKNSTVNASQDVSLACHAEAYPANLTYSWFQDNINVFHISRLQPRVRILVDGSLRLLATQPDDAGCYTCVPSNGLLHPPSASAYLTVLYPAQVTAMPPETPLPIGMPGVIRCPVRANPPLLFVSWTKDGKALQLDKFPGWSQGTEGSLIIALGNEDALGEYSCTPYNSLGTAGPSPVTRVLLKAPPAFIERPKEEYFQEVGRELLIPCSAQGDPPPVVSWTKVGRGLQGQAQVDSNSSLILRPLTKEAHGHWECSASNAVARVATSTNVYVLGTSPHVVTNVSVVALPKGANVSWEPGFDGGYLQRFSVWYTPLAKRPDRMHHDWVSLAVPVGAAHLLVPGLQPHTQYQFSVLAQNKLGSGPFSEIVLSAPEGLPTTPAAPGLPPTEIPPPLSPPRGLVAVRTPRGVLLHWDPPELVPKRLDGYVLEGRQGSQGWEVLDPAVAGTETELLVPGLIKDVLYEFRLVAFAGSFVSDPSNTANVSTSGLEVYPSRTQLPGLLPQPVLAGVVGGVCFLGVAVLVSILAGCLLNRRRAARRRRKRLRQDPPLIFSPTGKSAAPSALGSGSPDSVAKLKLQGSPVPSLRQSLLWGDPAGTPSPHPDPPSSRGPLPLEPICRGPDGRFVMGPTVAAPQERSGREQAEPRTPAQRLARSFDCSSSSPSGAPQPLCIEDISPVAPPPAAPPSPLPGPGPLLQYLSLPFFREMNVDGDWPPLEEPSPAAPPDYMDTRRCPTSSFLRSPETPPVSPRESLPGAVVGAGATAEPPYTALADWTLRERLLPGLLPAAPRGSLTSQSSGRGSASFLRPPSTAPSAGGSYLSPAPGDTSSWASGPERWPRREHVVTVSKRRNTSVDENYEWDSEFPGDMELLETLHLGLASSRLRPEAEPELGVKTPEEGCLLNTAHVTGPEARCAALREEFLAFRRRRDATRARLPAYRQPVPHPEQATLL
|
Functions in dendrite outgrowth and synapse maturation.
|
Q9P2J2
|
Q21DB1
|
TSAD_RHOPB
|
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
|
Rhodopseudomonas
|
MATDTASLVLGIETTCDETAAAVVERRSDGSGRILSNIVHSQIEDHAPFGGVVPEIAARAHVDLLDGIIARAMQQAGLGFKDLSGVAAAAGPGLIGGVIVGLTTGKAIALVHDTPLIAVNHLEAHALTPRLTDALQFPYCLFLASGGHTQIVAVLGVGNYVRLGTTVDDAMGEAFDKVAKMLGLPYPGGPQVERAAAAGDAARFAFPRPMLGRADANFSLSGLKTAVRNEASRLSPLEPQDVNDLCAGFQAAALESTADRLHVGLRIFRERFGAPHALVAAGGVAANQAIRGALQQVALAAGTQFMIPPPALCTDNGAMIAWAGAERLALGLTDSLEFAPRARWLLDANVITPAQFANTRAGF
|
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
|
Q21DB1
|
A0Q5Q7
|
UVRC_FRATN
|
Excinuclease ABC subunit C
|
Francisella
|
MIVDNSKDFDLKSFLANLTTHSGVYRMLDKHGEIIYVGKAKNLKNRVNSYFSKGAKDSKTLMMVEQIARIEITITPSDYEAYLLENNLIKQHRPKYNILFKDDKSYPYLVISRDKFPRVSFYRGKSAYKKGQCFGPYVSISSVKNTLNTIQKIFPIRQCENSYYKSRVRPCLQYQIKRCLAPCVGLVSQQQYDEQLAILKKFLAGKFSTVLEEISAKMYQASEDMEYEKAQVYRDQLVVLRKLQQQQIVDIQEDKTFDVIGIYMQDSYASIALLQIQNGDVVADRHWSIDAKGQDKTSIMHAFLSHFYLGDEIRNIWPKNIILSKVEFADITDLMNSISQKIGQAINWIIAPAADNLKWLKLAEVNARQKLNIYTSSKSQYQKRLESLKEFLELEKDIKRIECFDISHFQGEATIASCVVYTDEGEDRKSHRRYNIKDIKAGDDYAAIYQAVSRRVSSGLEADNLPDVMIIDGGKGQIHQAEAVFREFGIQDKVQLVSLGKGVERISGKEKIYKGFDDTEYTLDEHNPGFLLLRQVRDSAHDHAIKGQRKKVSANRQSSIIEEIEGVGPKRRKALIMYFGGWQELSRASVDEIAKVKGISKKLAQEIWECFH
|
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
|
A0Q5Q7
|
Q822J3
|
TAL_CHLCV
|
Transaldolase
|
Chlamydia
|
MSSQFEQLKLLSVLVCDTGDPELVKTSGSQDATTNPSLILKVAQEPKYQELLTEAIAWGIRQNGDDIQTLTFVLDKIQVNFGLEILKCIPGRVSLEIDARLSFNTEAMIQRAIFLSELFAATGGDKKRLLVKIPGTWEGIRAVEVLEKQGIACNVTLIFNLIQAIAAAKANATLISPFVGRIYDWWIAAYGDEGYSIDADPGVASVSNIYTYYKKFDIPTQIMAASFRSKEQVLALAGCDLLTVSPKLLDELKKDQSPVAKKLDVAAAKKLDVQPVELTESVFRFLMNEDAMATEKLAEGIRIFSGDTQILEAAVTEFIKQIAAQDA
|
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
|
Q822J3
|
B1M3X4
|
UREG1_METRJ
|
Urease accessory protein UreG 1
|
Methylobacterium
|
MTSTNGPLRVGIGGPVGSGKTALMEQLCKRFRDRYEICAITNDIYTKEDARILTVAGALPEERILGVETGGCPHTAIREDASINLAAVAEMSRRFPKLDLVLIESGGDNLAATFSPELADITLYVIDVAGGEKIPRKGGPGITRSDLLIVNKTDLAPLVGADLSVMESDTQRMRGTRPYVFASLREGTGADAVARFVEEAGGLGR
|
Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG.
|
B1M3X4
|
Q21XE6
|
UPPP_ALBFT
|
Undecaprenyl pyrophosphate phosphatase
|
Rhodoferax
|
MDIVLLIKAAIMGLVEGLTEFLPISSTGHLILAGTLLGFDNEVGKVFDIAIQTGAIFAVILVYWQKIRDTLVALPTEKQAQRFSLNVLIAFVPAVVLGLLFGKAIKAHLFTPVVVASTFIIGGFIILWAERRQEKNPAAVRIHDVESMTPMDALKVGLAQCLAMIPGTSRSGATIIGGMLLGLSRKAATDFSFYLAIPTLIGAGVYSLFKERALLSMADLPTFAVGLVVSFFSAWLCIRWLLRYIASHSFVGFAYYRIVFGVVVLATAWSGAVTWAA
|
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
|
Q21XE6
|
P12058
|
TRAL_SALTI
|
Protein TraL
|
Salmonella
|
MEGNDLDKYRFPKTLSEQNRIIGLPLDEAIPAAVVLLWGFFTKKYLFSLIIAAVIWQLIRAAKCGKSSRWLYNWCYWYLPTELFRVVYRVIPDSSFRKWIK
|
Membrane protein involved in F pilin formation.
|
P12058
|
P10858
|
YADA_YERPS
|
Type 5 secretion system autotransporter YadA
|
Yersinia
|
MTKDFKISVSAALISALFSSPYAFAEEPEDGNDGIPRLSAVQISPNVDPKLGVGLYPAKPILRQENPKLPPRGPQGPEKKRARLAEAIQPQVLGGLDARAKGIHSIAIGATAEAAKPAAVAVGAGSIATGVNSVAIGPLSKALGDSAVTYGASSTAQKDGVAIGARASASDTGVAVGFNSKVDAQNSVAIGHSSHVAADHGYSIAIGDLSKTDRENSVSIGHESLNRQLTHLAAGTKDNDAVNVAQLKKEMAETLENARKETLAQSNDVLDAAKKHSNSVARTTLETAEEHANKKSAEALVSAKVYADSNSSHTLKTANSYTDVTVSSSTKKAISESNQYTDHKFSQLDNRLDKLDKRVDKGLASSAALNSLFQPYGVGKVNFTAGVGGYRSSQALAIGSGYRVNESVALKAGVAYAGSSNVMYNASFNIEW
|
Collagen-binding outer membrane protein forming a fibrillar matrix on the bacterial cell surface. Promotes attachment to eukaryotic cells and after invasion, is the major adhesin in infected tissue. Constitutes an alternative uptake pathway under conditions in which invasin synthesis is repressed.
|
P10858
|
Q7SIC9
|
TKTC_MAIZE
|
Transketolase, chloroplastic
|
Zea
|
GAVETLQGKAATGELLEKSVNTIRFLAIDAVEKANSGHPGLPMGCAPMGHVLYDEVMRYNPKNPYWFNRDRFVLSAGHGCMLQYALLHLAGYDSVKEEDLKQFRQWGSRTPGHPENFETPGVEVTTGPLGQGIANAVGLALAEKHLAARFNKPDSEIVDHYTYVILGDGCQMEGIANEACSLAGHWGLGKLIAFYDDNHISIDGDTEIAFTEDVSTRFEALGWHTIWVKNGNTGYDDIRAAIKEAKAVTDKPTLIKVTTTIGFGSPNKANSYSVHGSALGAKEVEATRQNLGWPYDTFFVPEDVKSHWSRHTPEGAALEADWNAKFAEYEKKYADDAATLKSIITGELPTGWVDALPKYTPESPGDATRNLSQQCLNALANVVPGLIGGSADLASSNMTLLKMFGDFQKDTAEERNVRFGVREHGMGAICNGIALHSPGFVPYCATFFVFTDYMRGAMRISALSEAGVIYVMTHDSIGLGEDGPTHQPIEHLVSFRAMPNILMLRPADGNETAGAYKVAVLNRKRPSILALSRQKLPHLPGTSIEGVEKGGYTISDNSTGNKPDLIVMGTGSELEIAAKAADELRKEGKTVRVVSFVSWELFDEQSDEYKESVLPAAVTARISIEAGSTLGWQKYVGAQGKAIGIDKFGASAPAGTIYKEYGITVESIIAAAKSF
|
Catalyzes the reversible transfer of a two-carbon ketol group from fructose-6-phosphate or sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate to yield xylulose-5-phosphate and erythrose-4-phosphate or ribose-5-phosphate, respectively.
|
Q7SIC9
|
Q5E4I0
|
TORD_ALIF1
|
Chaperone protein TorD
|
Aliivibrio
|
MNELTAFNEQRAEIYWWLSSLLSAELTTEQLEQYGSFEVRTFLSNLAETPELSDSVNALIEKLNAVQGREDAQLELSADFCDAFLGSDKSSALPYASMYLDKSGLLNAKPAQDMREWLTKYNIAQKAEFNEPADHIAIELDFLGNLIVMTNQQVSEDEFEAYMSAQLTFINEQLLSWTPRFNEICIERDKFGFYAAVTGLLVTFLKLDVKFLAGE
|
Involved in the biogenesis of TorA. Acts on TorA before the insertion of the molybdenum cofactor and, as a result, probably favors a conformation of the apoenzyme that is competent for acquiring the cofactor.
|
Q5E4I0
|
Q5HBS1
|
TATA_EHRRW
|
Sec-independent protein translocase protein TatA
|
Ehrlichia
|
MALGPWQIFLILVIILVLFGAGKLPDVMSDLGKGIRNLKQELKDNKLASTEDESNL
|
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.
|
Q5HBS1
|
B6DCT7
|
TX405_LYCSI
|
Toxin-like structure LSTX-C5
|
Lycosa
|
MKVLVLFSVLFLTLFSYSSTEAMDEFDSDAEEDMLSLMANEQVRAKACTPRLHDCSHDRHSCCRGELFKDVCYCFYPEGEDKTEVCSCQQPKSHKYIEKVVDKARTVVG
|
Enhances the high-affinity desensitization of human P2RX3 purinoceptors.
|
B6DCT7
|
Q4P235
|
TBB_USTMA
|
Beta-tubulin
|
Ustilago
|
MREIVHLQTGQCGNQVGTKFWEVLSDEHGIDHNGNYIGTSDDQLARINVYYNEASGNKYVPRAVLVDLEPGTMDSTRSGPLGGLFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVIRKEAENCDMLQGFQITHSLGGGTGAGMGTLLISKIREEYPDRMMATFSVLPSPKVSDTVVEPYNATLSVHQLVENSDETFCIDNEALYNICFKTLKLNAPTYGDLNHLVSLVMSGVTTCLRFPGQLNSDLRKLAVNMVPFPRLHFFMVGFSPLTARGSQSYRAVTIPEITQQAFDSKNMMTACDTRLGRYLTCAAYFRGKVSMKDVEDQMQSFQQKHSTQFVEWIPNNVQTAQCDIPPRGLKMSVTFIGNSTAIQDVFKRIAEQFSAMFKRKAFLHWYTGEGMDEMEFTEAESNLQDLIAEYQQYQDASALDEDIEGEYIEEEELVQE
|
Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
|
Q4P235
|
Q10424
|
ZIP1_SCHPO
|
Transcription factor zip1
|
Schizosaccharomyces
|
MDFTPNSAINHLNLKFDDVPVSDDFSKDDLAEQLNVFTNPYFLDLEPSSMLSEGYYGFVSQPSGSSNSNKQEKNVQQQNPEKISTLQQVKEEEVSNTFSAPLNATGNFSSANPASIDLAYLDLQKLLTLPDHSKETQEKTSSQRELFEQKSSVASASKDNVSSSSILQGSASSKLLPDQSARQHQVLVGQTAIPTSEASSSINNTPLQAPVSSFADQNAFTNPLSTFASPDLASVSSPSLSSYKGAQSPNANSKRTKATSAIRTAAEEDKRRRNTAASARFRIKKKLKEQQLERTAKELTEKVAILETRVRELEMENNWLKGLIRPTSNF
|
Mediates cell growth arrest in response to cadmium exposure, which is essential to maintain cell viability. Regulates cadmium stress specific genes.
|
Q10424
|
A0Q5K3
|
TDH_FRATN
|
L-threonine 3-dehydrogenase
|
Francisella
|
MKALAKLKKQPGIWMIDDAPIPEYGYNDVLIKIKKTAICGTDLHIYNWDKWSQNTIPVPMITGHEFAGEVVAKGDGVTSVDIGDRVSGEGHLVCGQCRNCRAGKRHLCRKTIGIGVNVQGAFAEYLVMPAVNVFKIPDSISDDIASTFDPMGNAIHTALSFNLTGEDVLITGAGPIGLMAVKIARFCGARRIVITDINEYRLQMARDFGATVALNVAPFKNQDELVKQMRKVMSDIGMTEGFDIGLEMSGINSAISMMLDVMNHGGKLSLLGISAGDISVDWGAILFKGLTLKGIYGREMFETWYLMTSMLQAGMDMNPIITHRLHIDEFQKGFEIMKSGQCGKVILDWSS
|
Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate.
|
A0Q5K3
|
A4VPB2
|
UPP_PSEU5
|
UPRTase
|
Pseudomonas
|
MPIREIRHPLIRHKLGLMRRADISTKNFRELAQEVGSILTYEATSDLPLEHYNIDGWCGPVQVEKISGKKITVVPILRAGIGMLDGVLSLIPGAKVSAVGIARNEETFKAQTYLEKLVPEIEQRLAIIIDPMLATGGSMVATIDMLKKAGCKEIRALVLVAAPEGIAAVEAAHPDVLILTASIDERLDEHGYIVPGLGDAGDKIFGTKQKDI
|
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
|
A4VPB2
|
Q7U845
|
YQGF_PARMW
|
Putative pre-16S rRNA nuclease
|
Parasynechococcus marenigrum
|
MPRPCSVLSLDVGRKRIGLAGCDPLGITVTPIKALHRGRFDDDLPVLQQLCQDRRVQGLVVGLPLDAAGQPTAQADHCLRYGRRLAQALQLPLAWVNEHSSTWAAGERHGLKGDRSGRLDSAAAALLLDQWLREGPDLKPVQGLLGGAGAELVDGGS
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
|
Q7U845
|
A8F4P7
|
UVRC_PSELT
|
Excinuclease ABC subunit C
|
Pseudothermotoga
|
MDLLHKAKLAPLLPGVYIFYGKNKEYIYVGKAKRLRNRLLSYFNRSNGKYSKKIQAIVNEAEELDYIVVSNEREALLLEANLIFNHKPKYNVMLKDAEFYPYIEITKELFPAVQIVRIRSTGGEYFGPYTDVKFVKDLIDCLQQVYQFRTCRRDMSKSTKPCMEFYMHRCAAPCTGDLEPDSYINSSIQPLRRVLNGDISETLDLIEEKMKKHAKMMDFENAAKYRDLLVKFENVMQRQGVVLEQWRNLDVIGRFKNSYAVLRIRGGHVVGKLSYELDSTKLEDFIFHYYMVGKNELPEAVILERNINFDAEIYFGRPRDKLEEELLHKARENAKNQAYTSGLRKDLLNKMVKVLNLNRYPMKIEGFDVSHLHGKLTVASVVVFFDGLPRKNEYRHYRFNSDRIDDFLTLKELVKRRYSKHELPDMIFVDGGTGQINAVVEALMEIGKECDVVGLAKQNEIVCTRFGELILPFDSPILRTLVRIRDEAHRFANSFHRKLRRKSALSSILDEIPGIGPKRKKKLIEAFGSVKNIRSATLQEIAEVLGSRKLAAEILSRL
|
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
|
A8F4P7
|
B6I6D5
|
TRUD_ECOSE
|
tRNA-uridine isomerase D
|
Escherichia
|
MIEFDNLTYLHGKPQGTGLLKANPEDFVVVEDLGFEPDGEGEHILVRILKNGCNTRFVADALAKFLKIHAREVSFAGQKDKHAVTEQWLCARVPGKEMPDLSAFQLEGCQVLEYARHKRKLRLGALKGNAFTLVLREVSNRDDVEQRLIDICVKGVPNYFGAQRFGIGGSNLQGALRWAQTNTPVRDRNKRSFWLSAARSALFNQIVAERLKKADVNQVVDGDALQLAGRGSWFVATTEELAELQRRVNDKELMITAALPGSGEWGTQREALAFEKAAVAAETELQALLVREKVEAARRAMLLYPQQLSWNWWDDVTVEIRFWLPAGSFATSVVRELINTTGDYAHIAE
|
Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
|
B6I6D5
|
Q06466
|
TDA6_YEAST
|
Topoisomerase I damage affected protein 6
|
Saccharomyces
|
MHCVLARILLWFLIVDLSVIRALVLPPLKDYDPLEPLMKRDMAMGQRNRFKVDGQLPPILNSTDVTDDQRSLHTPGEIPSYVINHCPLVHLYSEEKYWPSDIAEYVQNFQIKDKNGNSISTHENLTLHDLKAEYHVDLFGNKTETHIPSSEVFLTSLDDFDKDPKWLLGHLPEYGTGYNSKAPAILIVVDKGNGWVDAFWFFFYPFNHGPFIMGHGPWGNHVGDWEHSLVRFYKGIPKYLWMSAHSSGTGYRYEAVEKFKKLRKRKQQDSDDGGDTILERPLIFSARGTHANYASAGQHAHDIPFFFMPLSDFTDRGPLWDPSLNFYSYTFDGKTVTPSSEREESLGLDWLHFQGGWGDQQLPARDPRQKWCVAQWKYIGGPRGPLFKKLDRLNLCGGVKKWNFWNGGCPARRLIKKAEGLDSESTDLMGDNCGVLLYRIRPKWLRGILRFLMWRGILCSLMEFFTN
|
Involved in vacuolar protein sorting.
|
Q06466
|
Q58E77
|
WD82B_XENLA
|
WD repeat-containing protein 82-B
|
Xenopus
|
MKLTDNVLRSFRVAKVFRENSDKINCFDFSPTGETVISSSDDDSIVLYDCQEGKPKRTLYSKKYGVDLIRYTHAANTVVYSSNKIDDTIRYLSLHDNKYIRYFPGHSKRVVSLSMSPVDDTFISGSLDKTIRLWDLRSPNCQGLMHLQGKPVCSFDPEGLIFAAGINSEMVKLYDLRSFDKGPFATFKMQYDRTCEWTALKFSNDGKLILLSTNGGFLRLVDAFKGAVMHTFGGYNNSKAVTLEASFTPDSQFIMIGSEDGKIHVWNCESGMKVAVLDGKHTGPITCLQFNPKFMTFASACSNMAFWLPTIDD
|
Regulatory component of the SET1 complex implicated in the tethering of this complex to transcriptional start sites of active genes. Facilitates histone H3 'Lys-4' methylation (H3K4me) via recruitment of the SETD1A or SETD1B to the 'Ser-5' phosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (POLR2A). Part of a transcription termination checkpoint that promotes transcription termination of long non-coding RNAs (lncRNAs).
|
Q58E77
|
Q65W23
|
YIHI_MANSM
|
Der GTPase-activating protein YihI
|
Basfia
|
MSRQKKSRNIVDVMPQRKSDKSQISPASYARPSKKLTRYELDAKAREDKKKKKHKGLTSGSRHSRSEQHNNQQMQEKRDPRLGSRKKVPLVVEFVNNPEKGQFIQPVQVQPAEEKVKKLDPMLELEQLENNECLNQLLDALDEGKTISAEDQKFVDECLDRIAQLMDELGIEDEEESEDDLLRTFEKIDINQFK
|
A GTPase-activating protein (GAP) that modifies Der/EngA GTPase function. May play a role in ribosome biogenesis.
|
Q65W23
|
Q94DG6
|
ZIP1_ORYSJ
|
ZRT/IRT-like protein 1
|
Oryza sativa
|
MARTMTMRVSSLLVAVVLLAALSFQACSGHGGINDGDGQVDAPATPASSSGVRSKGLIAVKVWCLVILLVFTFAGGVSPYFYRWNESFLLLGTQFAAGVFLGTALMHFLADSTSTFKGLTTNQYPFSFMLTCVGFLLTMLSDLVIAAVARRSAAAGVSDNQVSEQQQRQQAEGAVMSRKEEEAAAVAHPAMLVRTSSFEDAVLLIVALCFHSVFEGIAIGVSASKSEAWRNLWTIGLHKIFAAVAMGIALLRMIPKRPFLMTVVYSLAFAVSSPVGVGIGIAIDATSQGRAADWTYAISMGLATGVFIYVAINHLIAKGYRPHHPTAADKPLFKFLAVLLGVAVMAVVMIWD
|
Zinc transporter that may mediate zinc uptake from the rhizosphere. May also transport other divalent cations.
|
Q94DG6
|
C4ZTI0
|
THII_ECOBW
|
tRNA 4-thiouridine synthase
|
Escherichia
|
MKFIIKLFPEITIKSQSVRLRFIKILTGNIRNVLKHYDETLAVVRHWDNIEVRAKDENQRLAIRDALTRIPGIHHILEVEDVPFTDMHDIFEKALVQYRDQLEGKTFCVRVKRRGKHDFSSIDVERYVGGGLNQHIESARVKLTNPDVTVHLEVEDDRLLLIKGRYEGIGGFPIGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGGAAHEIGVRQVAHYLWNRFGSSHRVRFVAINFEPVVGEILEKIDDGQMGVILKRMMVRAASKVAERYGVQALVTGEALGQVSSQTLTNLRLIDNVSDTLILRPLISYDKEHIINLARQIGTEDFARTMPEYCGVISKSPTVKAVKSKIEAEEEKFDFSILDKVVEEANNVDIREIAQQTEQEVVEVETVNGFGPNDVILDIRSIDEQEDKPLKVEGIDVVSLPFYKLSTKFGDLDQNKTWLLWCERGVMSRLQALYLREQGFNNVKVYRP
|
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.
|
C4ZTI0
|
Q108P1
|
TNMT_PAPSO
|
(S)-tetrahydroprotoberberine N-methyltransferase
|
Papaver
|
MGSIDEVKKESAGETLGRLLKGEIKDEELKKLIKFQFEKRLQWGYKSSHQEQLSFNLDFIKSLKKMEMSGEIETMNKETYELPSEFLEAVFGKTVKQSMCYFTHESATIDEAEEAAHELYCERAQIKDGQTVLDIGCGQGGLVLYIAQKYKNCHVTGLTNSKAQVNYLLKQAEKLGLTNVDAILADVTQYESDKTYDRLLMIEAIEHMKNLQLFMKKLSTWMTKESLLFVDHVCHKTFAHFFEAVDEDDWYSGFIFPPGCATILAANSLLYFQDDVSVVDHWVVNGMHMARSVDIWRKALDKNMEAAKEILLPGLGGSHETVNGVVTHIRTFCMGGYEQFSMNNGDEWMVAQLLFKKK
|
Involved in the biosynthesis of protopine and benzophenanthridine alkaloids. Catalyzes the conversion of the protoberberine alkaloids stylopine, canadine, and tetrahydropalmatine to their corresponding N-methylated derivatives. No activity with dimethoxytetrahydroisoquinoline, methylisoquinolinediol, norlaudanosoline, (R,S)-tetrahydroxyberbine, (S)-scoulerine or (R,S)-pavine as substrates.
|
Q108P1
|
A3NXK5
|
UVRC_BURP0
|
Excinuclease ABC subunit C
|
pseudomallei group
|
MTSPDAPESRFEPKPILAQLPHLPGVYRYYDAQDAVLYVGKARDLKKRVSSYFTKTQLSPRIAMMITRIARIETTVTRSEAEALLLENNLIKALAPRYNILFRDDKSYPYLKLTGHRFPRMAYYRGAVDKKNQYFGPFPSAWAVRESIQILQRVFQLRTCEDSVFNNRTRPCLLHQIGRCSAPCVGAIGEEDYARDVDNASRFLLGRQGEVMGELERKMHAFAAELKFEQAAAVRNQMSSLAKVLHQQAIDVGGDSDVDILAVVAQGGRVCVNLAMVRGGRHLGDKAYFPAHVETALALAGDIEALAGEGAGDGVQAAAQPAQAPLATDADATDAAATEAKTVTAAAAARAGARTAQAAGARAAASAEGDVERRAEGETHARADAREAAALPDGAAAAQEADADVDAAPLETEVLEAFIAQHYLGNRVPPVLVVSHAPANRELIDLLVEQAGHKVAVVRQPQGQKRAWLTMAEQNARLALARLLSEQGSQQARTRSLADVLGYESDDLAQLRIECFDISHTMGEATQASCVVYHHHRMQSSEYRRYNIAGITPGDDYAAMRQVLTRRYEKMVEEAAAEASADEAAGIDGNAVHAAASAGRLPNVVLIDGGRGQVEIARQVFSELGLDISMLVGVAKGEGRKVGLETLIFADGRAPLELGKESAALMLVAQIRDEAHRFAITGMRAKRAKTRQTSRLEELEGVGAKRRQRLLARFGGLRGVVAASVDELASVEGISRALAEQIYRQLH
|
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
|
A3NXK5
|
B2U8Z0
|
UPP_RALPJ
|
UPRTase
|
Ralstonia
|
MKQDPRFPNLSILNHPLIQHKLTHMRDKDTSTRTFRELLREITLLMGYEITRNLPLTSRHIDTPMGPMEAPVIAGRKLAVVPVLRAGVGMSDGLVELIPSARIGHIGVYRDDQHRPVEYLVRLPDLEDRTFILCDPMVATGYSAVHAVDVMKKRGVPDENILFLALVAAPEGVEVFQKAHPGVKLFVASLDSHLDENAYIIPGLGDAGDRLFGTKN
|
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
|
B2U8Z0
|
P22275
|
TBA3_MAIZE
|
Alpha-3-tubulin
|
Zea
|
MRECISVHIGQAGIQVGNACWELYCLEHGIQPDGQVPGDKTAGHHDDAFSTFFSQTGAGKHVPRAIFVDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVEYGKKSKLGFTVYPSPQVSTSVVEPYNSVLSTHSLLEHTDVSILLDNEAIYDICRRSLDIERPNYSNLNRLVSQVISSLTASLRFDGALNVDVNEFQTNLVPYPRIHFMLSSYAPVISSAKAFHEQLSVAEITSSAFEPASMMVKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKRTIQFVDWCPTGFKCGINYQAPTVVPGADLAKVQRAVCMISNSTSVVEVFSRINSKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVAAEGGSDDGDEEEEY
|
Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
|
P22275
|
Q3K9H0
|
TAL_PSEPF
|
Transaldolase
|
Pseudomonas
|
MTSKLEQLKQFTTVVADTGDFEAIARVKPVDATTNPSLLLKAAAIPAYAELLNASVRDCKGDVGLASDRFGVAVGQEILKVIPGRISTEVDARLSFDQDAVLKRAHRLIELYDKAGVGRDRVLIKIASTWEGIRAAEILEKEGIQTNLTLLFSFAQAAACADAGVFLISPFVGRIYDWYKKANGNDYTGADDPGVQSVTRIYNYYKANDYKTVVMGASFRNLSQIEQLAGCDRLTISPDLIEKLAADTGKLERKLAPGHAGEARLSLNEAQFRWLSNEDAMATEKLAEGIRQFARDQEKLEALLQAKL
|
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
|
Q3K9H0
|
A0M5T6
|
UPPP_GRAFK
|
Undecaprenyl pyrophosphate phosphatase
|
Gramella
|
MDIFDAIVLGIIQGLTEFLPVSSSGHLELGKAILGDTSLPEESLLFTVVLHFATALSTLVVFRKDVFEIFSGLLKFKWNEETQFSLKIIISMLPAVIVGLLFEEQLEALFGGNILFVGFMLLITALLLWLADKAKDTGKKVSYRNAFIIGVSQAIAMLPGISRSGATISTSVLLGNDKTKAARFSFLMVVPLIFGKIAKDLMSGELMASSTDFSILATGFIAAFLAGLVACTWMISLVKKSKLSWFAIYCFVVGLAAIIFAYAQ
|
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
|
A0M5T6
|
A0JYP1
|
THIE_ARTS2
|
Thiamine-phosphate pyrophosphorylase
|
Arthrobacter
|
MTEQALLTDARLYLCTDARTDRGDFADFVDAAYAGGVDIIQLRDKGLEAAEELELLEVLETAARRHGRLWSVNDRADIASLSGAPVLHVGQKDLPLASARKFLGGEAVIGLSTHSHGQIDAAIAASRGAGGLDYFCVGPVWATPTKPGRAAVGLELVRYAAEAAGKTTAKTTGGAAGPTVDGPRLPWFAIGGIDLGNVEQVAAAGAERIVVVRAITEADDPAAAARSLLAALDAGAS
|
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
|
A0JYP1
|
P29172
|
TAU_BOVIN
|
Paired helical filament-tau
|
Bos
|
MAEPRQEFDVMEDHAQGDYTLQDQEGDMDPGLKESPLQTPADDGSEEPGSETSDAKSTPTAEDATAPLVDEGAPGEQAAAQAPAEIPEGTAAEEAGIGDTSNLEDQAAGHVTQARMVSKGKDGTGPDDKKTKGADGKPGTKIATPRGAAPPGQKGQANATRIPAKTTPTPKTSPATMQVQKKPPPAGAKSERGESGKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSAAKSRLQAAPGPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL
|
Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by tau localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization.
|
P29172
|
Q0HMG7
|
Y670_SHESM
|
Nucleotide-binding protein Shewmr4_0670
|
Shewanella
|
MKLVIVSGRSGSGKSVALRVLEDLGYYCVDNLPLPLIGSLLEQLKGSNDLVAISVDVRNLPEQDKVLVKQLTSLPEGTELTSFFLNSSDKVLLKRYSETRRLHPLSKSRVSLQEAIKLEGKLLEPLSQQMDHYIDTSNLNIYELSDQVRQILLGSVDKELVINFESFGFKHGMPTEADFMFDVRFLPNPHWEPELRPLTGLDEPVAEFLNRQPLVNKFIWQIENLLETWLPHLERNNRSYLTIAIGCTGGQHRSVYVAEQLAKRFSNGKHKVNARHRELSHAKA
|
Displays ATPase and GTPase activities.
|
Q0HMG7
|
Q4P0L3
|
XY11A_USTMA
|
1,4-beta-D-xylan xylanohydrolase 11A
|
Ustilago
|
MKFATVLAFATAAGAAFASPLASSETTEAGQLSKRQSINYVQNYNGNAANFKYDQHAGTYSTRWTNPPDFVVGLGWSPGNSYRTIKFSGSYSSSSSSYSAVYGWLNNPLTEYYVVENYSYDPCSNSGAQVVGSVTSDGSNYKICKHTQYDQPSIQGTKTFGQYFSVRANKRNSGSVTLSKHFNAWKQHGFANGAANPDFNYQVFATEAFGGTGSASMSVSG
|
Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.
|
Q4P0L3
|
B1MZE7
|
TRMB_LEUCK
|
tRNA(m7G46)-methyltransferase
|
Leuconostoc
|
MHLRAKPWATDWLAAHSDIVITQGRATEQIGQWQKLFAKAQPIHVEIGSGKGQFILGMALAHPEINYIGMEIQETAVAIAARKSFDQVGELPNLRYIYGNGNGVETYFEKAEVEKIYLNFSDPWPKTRHESRRLTYKTFLQSYEAVLPEHGEVEFKTDNRHLFEYSIVSFMNYGMRWATTDFTLDLHADAEKVIGNVETEYEQKFMAKGQPIYKIKAHF
|
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
|
B1MZE7
|
Q02F45
|
THIC_PSEAB
|
Thiamine biosynthesis protein ThiC
|
Pseudomonas
|
MSATQKNNITRLEQLDRQSTQPFPNSRKVYLTGSRPDIRVPVREISLADTPTAFGGEKNPPVFVYDTSGPYTDPEVRIDLRKGLPDVRSRWIDERGDTEILPGLTSEFGQARLADASLDALRFAHVRTPRRAKPGANVSQMHYAKKGIITPEMEYIAIRENMKLQEARAAGLLDQQHPGHSFGANTPKEITPEFVREEVARGRAIIPANINHTELEPMIIGRNFLVKINGNIGNSALGSSIEEEVEKLTWGIRWGADTVMDLSTGKHIHETREWILRNSPVPIGTVPIYQALEKVNGVAEDLTWEIFRDTLIEQAEQGVDYFTIHAGVLLRYVPLTAKRVTGIVSRGGSIMAKWCLAHHQENFLYTHFEEICEIMKAYDVSFSLGDGLRPGSVADANDAAQFGELETLGELTKIAWKHDVQVMIEGPGHVPMQLIKENMDKQLECCDEAPFYTLGPLTTDIAPGYDHITSGIGAAMIGWFGCAMLCYVTPKEHLGLPNKDDVKTGIITYKIAAHAADLAKGHPGAQIRDNALSKARFEFRWEDQFNLGLDPDTARAFHDETLPKDSAKVAHFCSMCGPKFCSMKITQEVRDYAKENGLSDESKAIEAGFQEQAARFKDEGSVIYRQV
|
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.
|
Q02F45
|
Q4AA71
|
TMCAL_MESHJ
|
tRNA(Met) cytidine acetate ligase
|
Mesomycoplasma
|
MAIAIIAEYNPFHNGHIYQLEYTKKNFPNDKIYIILSGNFTQRGEISLADFKTKSKIALKYGADFIIKLPFEYATQAAHIFAKGAIKIVNQHKIDKIIFGSESNDVENLYKLANLWNQNQEAYNAFLKYALKLGYSFPKASAFALEEISGQKIVFPNDILGFEYIKQIVANNYPIRAYTLKRSEEFSLKNPEPNIASATYLRQLVNENKSISRFSPMKFIHPVCSLANLYPEFQKIVRETSPENLAKIWLISEGIENLFKKHINEPNFEKFLNAVNSRRYTNSRIKRAMVYILFRIEDPSQFDEEKIQLDCWKNQGF
|
Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
|
Q4AA71
|
B0TYR8
|
TDH_FRAP2
|
L-threonine 3-dehydrogenase
|
Francisella
|
MKALAKLKKEPGIWMIDDAPMPEYGYNDVLIKIKKTAICGTDLHIYNWDKWSQATIPVPMITGHEFAGEVVAKGNGVTSVDVGDRVSGEGHLVCGQCRNCRAGKRHLCRKTIGIGVNVQGAFAEYLVMPAVNVFKIPDSISDDIASTFDPMGNAIHTALSFNLTGEDVLITGAGPIGLMAVKIARFCGARRIVITDINKYRLQMARDFGATVAVNVSEFQNQQQLTAQMRKVMSEIGMTEGFDVGLEMSGINSAISMMLDVMNHGGKLSLLGISAGDISVDWGAILFKGLTLKGIYGREMFETWYLMTSMLQAGMDMEPIITHRLHIDDYQKGFEIMKSGQCGKVILDWSR
|
Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate.
|
B0TYR8
|
Q8IWU4
|
ZNT8_HUMAN
|
Solute carrier family 30 member 8
|
Homo
|
MEFLERTYLVNDKAAKMYAFTLESVELQQKPVNKDQCPRERPEELESGGMYHCHSGSKPTEKGANEYAYAKWKLCSASAICFIFMIAEVVGGHIAGSLAVVTDAAHLLIDLTSFLLSLFSLWLSSKPPSKRLTFGWHRAEILGALLSILCIWVVTGVLVYLACERLLYPDYQIQATVMIIVSSCAVAANIVLTVVLHQRCLGHNHKEVQANASVRAAFVHALGDLFQSISVLISALIIYFKPEYKIADPICTFIFSILVLASTITILKDFSILLMEGVPKSLNYSGVKELILAVDGVLSVHSLHIWSLTMNQVILSAHVATAASRDSQVVRREIAKALSKSFTMHSLTIQMESPVDQDPDCLFCEDPCD
|
Facilitates the accumulation of zinc from the cytoplasm into intracellular vesicles, being a zinc-efflux transporter. May be a major component for providing zinc to insulin maturation and/or storage processes in insulin-secreting pancreatic beta-cells.
|
Q8IWU4
|
Q72D63
|
XGPT_DESVH
|
Xanthine phosphoribosyltransferase
|
Desulfovibrio
|
MSTADRYRKVFPVTWEQLHRDAKALSWRLLEKGPYKGIIAIARGGLVPAAVIARELDIHLVETICISSYQWQEQTSSHKVLKTVEGRGEGWLIIDDLADTGGTARLVREMLPEAHFATVYAKPAGRPLVDTFITEVSQDTWILFPWDSEVQYVVPLVNQPQQS
|
Purine salvage pathway enzyme that catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to the N9 position of the 6-oxopurines guanine and xanthine to form the corresponding ribonucleotides GMP (guanosine 5'-monophosphate) and XMP (xanthosine 5'-monophosphate), with the release of PPi. To a lesser extent, also acts on hypoxanthine.
|
Q72D63
|
B5F4F0
|
TREA_SALA4
|
Alpha,alpha-trehalose glucohydrolase
|
Salmonella
|
MIPPEIRRSVLLQKAIKLALAGTLLTFASFSATAADPSSDTETPQPPDILLGPLFNDVQNAKLFPDQKTFADAIPNSDPLMILADYRMQRNQSGFDLRHFVDVNFTLPKAGEKYVPPAGQSLREHIDGLWPVLTRSTKNVEKWDSLLPLPESYVVPGGRFREIYYWDSYFTMLGLAESGHWDKVADMVANFGYEIDAWGHIPNGNRTYYLSRSQPPFFAFMVELLAQHEGDDALKEYLPQLQKEYAYWMEGVETLQPGQQNQRVVKLEDGSVLNRYWDDRDTPRPESWVEDIATAKSNPNRPATEIYRDLRSAAASGWDFSSRWMDNPQQLSTIRTTTIVPVDLNALLYQLEKTLARASAAAGDRAKASQYDALANARQKAIEMHLWNNKEGWYADYDLQNNKIRNQLTAAALFPLYVNAAAKDRAAKVAAAAQAHLLQPGGLATTSVKSGQQWDAPNGWAPLQWVAAEGLQNYGQDDVAMEVTWRFLTNVQHTYDREKKLVEKYDVSSTGTGGGGGEYPLQDGFGWTNGVTLKMLDLICPQEKPCDSVPSTRPASLSATPTKTPSAATQ
|
Provides the cells with the ability to utilize trehalose at high osmolarity by splitting it into glucose molecules that can subsequently be taken up by the phosphotransferase-mediated uptake system.
|
B5F4F0
|
Q2YIT7
|
VIRB3_BRUA2
|
Type IV secretion system protein virB3
|
Brucella
|
MTTAPQESNARSAGYRGDPIFKGCTRPAMLFGVPVIPLVIVGGSIVLLSVWISMFILPLIVPIVLVMRQITQTDDQMFRLLGLKAQFRLIHFNRTGRFWRASAYSPIAFTKRKRES
|
The virB operon is essential for intracellular survival and is not involved in the invasion process. Constitutes a major determinant of virulence in mice.
|
Q2YIT7
|
E7FEV0
|
WDR81_DANRE
|
WD repeat-containing protein 81
|
Danio
|
MEWLAPALERDLGIDQRQTAHSQRPNELVVLVPTRWVMALRNKRVTRCAKYESFSEGEICTLLQRSQMKLPSGWTRVCIQGLRKRKLGYRFARETGCHGEGLSQDSFMTLMQGVSQSNFRNLWHEAYMTHVQPYADSVEQTPVLALDAVRQALQKLFCSNFISTDRVSPSLSPAKEKEKDCPFLSTCSAPKQSTESLCPNVLPAECLLESEEVLYVVFPYTQYTVHDIVTYSPAKLANSNAKILFILYQLLIAMRECHASGLLCGELSLLDIAVDEQLCSRLKISLAHYEKFKEYRDAVPYALQNKVPMSVSTKDNHNNGVSGQLCRNCQDELKSLVLDWVNGQVSNFQYLMELNRLAGRREGDPNYHPVLPWVVDFTVPYGRFRDLKKSKFRLNKGDKQLDFTYEMTKEALAAVSGSGGSNYPPDLGGPVVPGGPGQSDHLHVPHHISDVLSDITYYVYKARQTPKSVLCSHVRSQWEPNEYPASMERIQSWTPDECIPEFYRDPSIFRSIHPDMPDLDVPPWCNSYEEFIAVHRQLLESREVSQQLHHWIDLTFGYKLSGKEAIKAKNVCLHLVDNHTHLTSYGVVQLFDHPHPPRLALYQYAPPEPPHFGRVNVTTWQIPPLETTMDGVDGLVPEATGCESSGWSVVGRDEELEQAIEALDLSGSSSSTSASVSIPVVGSAAGKTSGETIGLVVSPSHGSFPGEATGNVTNTLGSGIRTAMLHRAASVSKKPEASNLEDFKISLPDGFKPLQPLEELEKLNTFLVKGLHSEIEHTMDLGINKKDLRSVPKVPLSFTDLFQRDMQALGVLIAEIFYSSKLRGLRPETHLRDRFQAVLKLCSTNLRDVPLPLHHALDTLLQVHKHCLKTETIIMHPQGLPFLFKYDPICEGLPPPNPWQLLSPIVSPLPFPEYFPTLHKFIFSYHSKMESINNIQGRDIVFNLWQQLETLLKGDITTEGLEILLPFVLSLMSEESTAVYAAWYLFEPVSRVLGPRNASKYLIKPLVGVYENPRCLRGRFYLYTDCFVLQLIVRLGLQVFLSSLLPHVLQVMTGFESCNTAAGTEWEGMKVLRGAAGALDEEEEEYECDDRRSSNATSSGKVGGGSGGGSGGVGVVGDQGLVDYSSGISLNDQVFLNEGEDFQNGFYVNNSASGATTVGTKQQNQSTANKDQDQESLSVGKLSDKSSASEVSIGDRASLKSADSSQDLKQASDGEDGGELEDEEETVEDREITVQRVPSLEMTLSVCTEESEATVATLEGDVMNGIVQEDGEKNMEEEETEHDPLEDSEEKEHKILLDTVCKTVRWLSAKLGPTLTSRFIARNLLRLLTSCYIGLDKHQFMLSVNEENSLECVGSVYEKKPVVGDQTARPVLECLIYIAHLYGEPVLTYQYLPYIGYLVSPPSSCRLNTRKEAGLLGAVVLTQKIIVFLSDTTLMDMLMKINQEVLLPLLDLLTSTKMGFPSGVQTRSAVCLKTLSLMALICLRIGREMVQQHMAETLSRFFQVFSLLQFLQNQIGSAPRREVAECTYLDLRIPDGAELTIELGVLEELQAVFNPEMAYASYIPFYCLIGDSGIRKLVTNHELVWSLAQSYHERASPGSPESNPVGGQRASAVGLSPSMGRQMSRSPFPAPSSTSTPLGGDILPESGTFGSHLVGNRIQVTRDTEACGSPNLSSLETWTHGRPYGSNAPPMSLATTALSSAGPSFSHSSYSWVMGPTPEDSALKQDLPRSSRSLQGNWLAYWQYEIGLNQQDSHFHFHQIRLQSFIGHSGTAKCLAPLAGEDYFLSGSKDKTVRLWPLYNHGDGTREVEPRLTYTEHRKSIFYVGQLEALQEVVSCDGTVHLWDQFTGKNIRCNEPLDGKNPITAVTTMPAPHCSVVFASADSVLRFIDPRKPGLQHEFRLAYSNLSAGLIRCLAVSPGGRTIAAGFSTGFIVLLDARTGLVLRGWPGHEGDILQMKAAEGNLLVSSSSDHTLTVWKDVEHKPLHQYRTPSDPIHAFDLYGAEIVAGTVANKIGVYSILDSTASLAGSTKLSTENFRGTLTSLSVLPTKRLLLLGSDNGAIRLLA
|
Functions as a negative regulator of the PI3 kinase/PI3K activity associated with endosomal membranes. By modifying the phosphatidylinositol 3-phosphate/PtdInsP3 content of endosomal membranes may regulate endosome fusion, recycling, sorting and early to late endosome transport. May also play a role in aggrephagy, the macroautophagic degradation of ubiquitinated protein aggregates. May also be involved in maintenance of normal mitochondrial structure and organization.
|
E7FEV0
|
Q9N5D6
|
UNC62_CAEEL
|
Uncoordinated protein 62
|
Caenorhabditis
|
MSGDSKVWAHASADTWAVQNGISTYDLDTSSIKREKRDHNEQFNDGYGPPPGSASADPASYIADPAAFYNLYTNMGGAPTSTPMMHHEMGEAMKRDKESIYAHPLYPLLVLLFEKCELATSTPRDTSRDGSTSSDVCSSASFKDDLNEFVRHTQENADKQYYVPNPQLDQIMLQSIQMLRFHLLELEKVHELCDNFCNRYVVCLKGKMPLDIVGDERASSSQPPMSPGSMGHLGHSSSPSMAGGATPMHYPPPYEPQSVPLPENAGVMGGHPMEGSSMAYSMAGMAAAAASSSSSSNQAGDHPLANGGTLHSTAGASQTLLPIAVSSPSTCSSGGLRQDSTPLSGETPMGHANGNSMDSISEAGDEFSVCGSNDDGRDSVLSDSANGSQNGKRKVPKVFSKEAITKFRAWLFHNLTHPYPSEEQKKQLAKETGLTILQVNNWFINARRRIVQPMIDQNNRAGRSGQMNVCKNRRRNRSEQSPGPSPDSGSDSGANYSPDPSSLAASTAMPYPAEFYMQRTMPYGGFPSFTNPAMPFMNPMMGFQVAPTVDALSQQWVDLSAPHE
|
Acts redundantly with ceh-20 and ceh-40 to perform overlapping roles during embryogenesis . Required for postembryonic development of the ectoderm, including the Q, V and P cell lineages, playing a crucial role in ensuring that these cells and their descendants undergo their invariant patterns of cell division, migration, fusion and morphogenesis . Has a role in the mig-13 pathway to promote anterior migration of neuroblasts in the Q lineage . Required for multiple roles in regulating vulva development . Associates with homeobox ceh-60 to regulate gene expression, including repression of genes involved in innate immunity and activation of genes involved in vitellogenesis . Involved in lipid homeostasis, contributing to the formation of the cuticle .
|
Q9N5D6
|
Q8SR76
|
TCPG_ENCCU
|
CCT-gamma
|
Encephalitozoon
|
MQKPIPRKMYILVPDKPAQIQNESAIAAKTISSVIRTCLGPRAMQKMVLTKINSIELTNDGNAILRELDVAHPSARSLIELAKTQDDEVGDGTTSVVLLAAEILNEMTYILDRDVHPIRICKALGRALEICIKAIDGAAISLDSNEETKIKIINGSVASKICNILKVPIGNLALEAVKKVYVKEENKCDLKNNMKVEKVLGGNLMESEVVDGVLINKDIIHPQMRRVIENPRIVIIESPLEYKKGESQTNYEFSKENDFTRALEIEEEQVREMCERIIGVRPDIVVCEKGISDLALSILFENNITGLRRLKKTDISRLSKVCGARSVSRPEDLEERHVGVSCGLFEYIKYGEEYYCKFSRCAHPKACSVVIRGPTKDILDELERNFMDAVKVAKSIFISPKLCPGGGAAEMAMAHELMQSAGDNEVEAEVFSRMASALTIIPSILLENSGVFNPLEAITLLEQKHKEGSFYGVNGTTGEIVDTRDLVLEPYAVKSQCIKSAVEAVSQLLRIDGIIESKR
|
Molecular chaperone; assists the folding of proteins upon ATP hydrolysis.
|
Q8SR76
|
A0AM40
|
Y2654_LISW6
|
Nucleoid-associated protein lwe2654
|
Listeria
|
MRGMGNMQGMMKQMQKMQKEMAKAQADLEVQEFTGTAGGGMVTVKATGKRVITDVVINEEVVDPEDIEMLQDLVLAATNDVLKQIEDTTSQTMGKFTQGLNLPGM
|
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
|
A0AM40
|
Q3J767
|
URED_NITOC
|
Urease accessory protein UreD
|
Nitrosococcus
|
MKKIAVFKQMPCEAADAPPAKTDLLPLSWPAKLELGYQRVKMRTVPVLRRHQGPLRVQKHLYPEGPAVCQHMILHPPGGIAGGDTLDIQIHAGSHAWAQLTSPGAAKWYRSEVSLARQNLALSTEPGGILEWLPQETIFFAGCQTALDTTIDLAEDAKVIAWDIIALGRPASGERFNSGRIYQRFRLRRNGRLLWSERMQLLGGSRLLESPIGFAGYPVAGTLLASGELNDQQLTACRSLPIEGGRGGLSQLPGLVVARFLGEETEAARNWFIALWQELRPALLGRSVSIPRIWNT
|
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
|
Q3J767
|
O29178
|
Y1087_ARCFU
|
Putative antitoxin AF_1087
|
Archaeoglobus
|
MPKIIEAVYENGVFKPLQKVDLKEGEKIRLRIEEGIADVIKEFSRKVDQDVLEEFLRERR
|
Possibly the antitoxin component of a type II toxin-antitoxin (TA) system.
|
O29178
|
Q9LZ03
|
TOP6A_ARATH
|
Protein ROOT HAIRLESS 2
|
Arabidopsis
|
MADKKKRKRSKDDEAEELPFKSILESDDVITELLKSYISSSIKAAAGAGGASSSSSKPLTLADLSLSSSCREVADLSLSSVQTEIETVIVQIARSILAGDGFSFSVPSRAASNQLYVPELDRIVLKDKSTLRPFASVSSVRKTTITTRILALIHQLCLRNIHVTKRDLFYTDVKLFQDQTQSDAVLDDVSCMLGCTRSSLNVIAAEKGVVVGRLIFSDNGDMIDCTKMGMGGKAIPPNIDRVGDMQSDAMFILLVEKDAAYMRLAEDRFYNRFPCIIVTAKGQPDVATRLFLRKMKMELKLPVLALVDSDPYGLKILSVYGCGSKNMSYDSANLTTPDIKWLGIRPSDLDKYKIPEQCRLPMTEQDIKTGKDMLEEDFVKKNPGWVEELNLMVKTKQKAEIQALSSFGFQYLSEVYLPLKLQQQDWL
|
Component of the DNA topoisomerase VI involved in chromatin organization and progression of endoreduplication cycles. Relaxes both positive and negative superturns and exhibits a strong decatenase activity. Involved in cell-elongation processes.
|
Q9LZ03
|
F8J4S0
|
TOP4A_OXYTA
|
Oxyopinin-4a
|
Oxyopes
|
MKISQVFIFVFLLMISVAWANEAYEEESNYLSERFDADVEEITPEFRGIRCPKSWKCKAFKQRVLKRLLAMLRQHAF
|
Disrupts cell membranes through the formation of pores (Probable). Has antibacterial activity against Gram-positive bacteria S.aureus (MIC=10 uM) and B.subtilis (MIC=0.5 uM) as well as Gram-negative bacteria P.fluorescens (MIC=1 uM) and E.coli (MIC=0.5 uM). Has hemolytic activity against human erythrocytes (EC(50)=7 uM).
|
F8J4S0
|
Q8K982
|
Y467_BUCAP
|
Nucleoid-associated protein BUsg_467
|
Buchnera
|
MFTKGGLGNLMKQAQQMQEKMAKVQEEIAKMEVTGEAGAGLVKVTINGAHNCRRVEVDPSLLKDDKDMLEDLAAAAFNDATRRISEVQKKKMSAISTGMQLPTGFNIPI
|
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
|
Q8K982
|
P19247
|
VVHA_VIBVU
|
Cytolysin
|
Vibrio
|
MKKMTLFTLSLLATAVQVGAQEYVPIVEKPIYITSSKIKCVLHTSGDFNATRDWCNAGASIDVRVNVAQMRSVQSATSDGFTPDAKIVRFTVDADKPGTGIHLVNELQQDHSWFQSWANRRTYIGPFASSYDLWVKPVSGYTPKKARDLPQNENKNYQHRDTYGYSIGINGKVGAEVNKDGPKVGGEVSGSFTYNYSKTLVFDTKDYRINNRSSLSDFDISFEREFGECDELRRQELGCYFTAAHWGSGWVFDKTKFNPISYSNFKPNYDVLYEAPVSETGVTDFEMGVKLNYRARFGTVLPSALFSVYGSAGSSTNSSTVKQRIRIDWNHPLFEAEAHVTLQSLSNNDLCLDVYGENGDKTVAGGSVNGWSCHGSWNQVWGLDKEERYRSRVASDRCLTVNADKTLTVEQCGANLAQKWYWEGDKLISRYVDGNNTRYLLNIVGGRNVQVTPENEANQARWKPTLQQVKL
|
Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture by mechanisms not clearly defined.
|
P19247
|
A8GLI7
|
YIHI_SERP5
|
Der GTPase-activating protein YihI
|
Serratia
|
MNQPSKAPRAPRSSAATPKNKKKSRAELDQEAREHKRAKKRRGLASGSRTQVESTNQKNKAAAQAKDPRIGSKVPVALVVEDKPKAKPQPKPKAEAKPKPRLTPEEELAKLENDERLDALLDRIDDGETLSAEDQKYVDQTLDRIDALMEQLGIELGDDDEEEEEKREDILKLLKGGNPKDVI
|
A GTPase-activating protein (GAP) that modifies Der/EngA GTPase function. May play a role in ribosome biogenesis.
|
A8GLI7
|
Q9A566
|
TRMFO_CAUVC
|
Folate-dependent tRNA(M-5-U54)-methyltransferase
|
Caulobacter
|
MTTNSTYQPVHVIGGGLAGSEAAWQIAQSGVPVILHEMRKDDATGKVITDAHQTDGLAEMVCSNSFRSDDWQFNAVGLLHAEMRKLGSLIMSCADQHQVPAGGALAVDRDGFSTEVTKRLSQHPLVTIVREEIAGLPPAPDGKNGWDNVIVATGPLTSPALAQAVLDLTGEGQLSFFDAIAPIIHFESINMDIAWRQSRYDKEGPGGDAAAYINCPMNKEQYEAFIDALLAGPKSEFKEWENVPYFDGCLPIEVMAERGRETLRHGPMKPVGLTNPRDPLVKAYAIVQLRQDNALGTLWNMVGFQTKLKHGVQAETFRMIPGLEDAQFARLGGLHRNTFINSPKLLDKSLRMKAQPRLRFAGQVTGVEGYVESAAMGLLTGRFAAADRKGAPIDAPPPTTALGALVEHITGGHLEAGNGPGSFQPMNINYGLLPPLEAPKVDEDGKKIPLKERGRAKKRLMSLRALKDLDAWMA
|
Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
|
Q9A566
|
Q570C8
|
THIK5_ARATH
|
Peroxisomal 3-oxoacyl-CoA thiolase 5
|
Arabidopsis
|
MERAMERQKILLRHLNPVSSSNSSLKHEPSLLSPVNCVSEVSPMAAFGDDIVIVAAYRTAICKARRGGFKDTLPDDLLASVLKAVVERTSLDPSEVGDIVVGTVIAPGSQRAMECRVAAYFAGFPDSVPVRTVNRQCSSGLQAVADVAASIRAGYYDIGIGAGVESMSTDHIPGGGFHGSNPRAQDFPKARDCLLPMGITSENVAERFGVTREEQDMAAVESHKRAAAAIASGKLKDEIIPVATKIVDPETKAEKAIVVSVDDGVRPNSNMADLAKLKTVFKQNGSTTAGNASQISDGAGAVLLMKRSLAMKKGLPILGVFRSFAVTGVEPSVMGIGPAVAIPAATKLAGLNVSDIDLFEINEAFASQYVYSCKKLELDMEKVNVNGGAIAIGHPLGATGARCVATLLHEMKRRGKDCRFGVISMCIGTGMGAAAVFERGDSVDNLSNARVANGDSH
|
Probably involved in long chain fatty-acid beta-oxidation prior to gluconeogenesis during germination and subsequent seedling growth. Involved in systemic jasmonic acid (JA) biosynthesis after wounding and may be during senescence.
|
Q570C8
|
B8IZH6
|
UPP_DESDA
|
UPRTase
|
Desulfovibrio
|
MAVYVVDHPLVRHKIGILRMESTSTSEFRSVSNEVARLLIYEATKGFRTEKHTVQGWAGPVEIEAISGKKVTVVPILRAGLGLMDGVLDMIPGAKISVVGLYRNEETLEPVEYYVKLASDMDQRLAIILDPMLATGGSLIATIELLKRHGCRQICSLNLVCAPEGIAKVEAAHPDVDIYTAAIDDHLNEQGYIIPGLGDAGDRIFGTK
|
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
|
B8IZH6
|
P36512
|
UDB13_RABIT
|
EGT10
|
Oryctolagus
|
MPVKCISVLLLLLQLSCCFSSGSCGKVLVWPMEFSHWMNMKTILDALVQQGHEVTVLRSSASIVIGSNNESGIKFETFHTSYRKDEIENFFMDWFYKMIYNVSIESYWETFSLTKMVILKYSDICEDICKEVILNKKLMTKLQESRFDVVLADPVSPGGELLAELLKIPLVYSLRGFVGYMLQKHGGGLLLPPSYVPVMMSGLGSQMTFMERVQNLLCVLYFDFWFPKFNEKRWDQFYSEVLGRPVTFLELMGKADMWLIRSYWDLEFPRPLLPNFDFIGGLHCKPAKPLPQEMEDFVQSSGEEGVVVFSLGSMISNLTEERANVIASALAQLPQKVLWRFEGKKPDMLGSNTRLYKWIPQNDLLGHPKTKAFITHGGANGVFEAIYHGIPMVGLPLFGDQLDNIVYMKAKGAAVKLNLKTMSSADLLNALKTVINDPSYKENAMTLSRIHHDQPMKPLDRAVFWIEYVMRHKGAKHLRVAAHDLTWYQYHSLDVIGFLLACVAITTYLIVKCCLLVYRYVLGAGKKKKRD
|
UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. Acts on small phenolic agents such as 2-beta-naphthol and 4-methylumbelliferone as well as bulky phenolic compounds like 2-hydroxy- and 4-hydroxybiphenyl. In contrast to 2B16 it is active toward octylgallate.
|
P36512
|
A5LGM7
|
TRET1_POLVA
|
Facilitated trehalose transporter Tret1
|
Polypedilum
|
MELNNKEDSPRHTVPFVRQITEDGKAKLEIYRPTTNPIYIYTQILAAIAVSMGSMVVGFASAYTSPALVSMQNTTITSFKVTEQEASWVGGIMPLAGLAGGIAGGPFIEYLGRKNTILATAVPFIVAWLLIAFANSIWMVLAGRALSGFCVGIASLSLPVYLGETVQPEVRGTLGLLPTAFGNIGILICFVAGKYVNWSGLAFIGSILPIPFMVLTLLIPETPRWFVTRGREERARKALQWLRGKKADVEPELKGIVKSHCEAERHASQNAIFDLMKRSNLKPLLIALGLMFFQQLSGINAVIFYTVSIFKDAGSTIDENLCTIIVGVVNFGATFFATVLIDRLGRKILLYISEVAMVITLLTLGTFFYYKNSGNDVSNIGWLPLASFVIYVIGFSSGVGPIPWLMLGEILPGKIRGSAASVATGFNWTCTFIVTKTFADIVAAIGNHGAFWFFGVICLIGLFFVIFFVPETQGKSLEEIERKMMGRVRRMSSVANMKPLSFNM
|
High-capacity facilitative transporter for trehalose, required to induce anhydrobiosis. Anhydrobiotic larvae can survive almost complete dehydration. Does not transport maltose, sucrose or lactose. Mediates the bidirectional transfer of trehalose. Responsible for the transport of trehalose synthesized in the fat body and the incorporation of trehalose into other tissues that require a carbon source, thereby regulating trehalose levels in the hemolymph.
|
A5LGM7
|
Q67ER8
|
TR116_RAT
|
Taste receptor type 2 member 33
|
Rattus
|
MNGVLYITFTVILSVEVIIGNFGNGIIALVNIMDLAKRRKISSVDQILTALAISRIVLLWLVLVSWWLSMFYPGQWMTEGIDVIVHNVWTTLNQISLWLATSFSVFCFLKVANFSNTIFFYLKIRVKKVMTGTLIMFLLLLGLNIIVINASKTILIPEYKVNMSNSLNLKNTQISMLFPFANTLFGFIPFAVSLVTFLLLFFSLWKHQRKMHHGAQGCRDSSTKAHIRVLQTLIASILLYFVFFLSLVVKVWISLFLERMLLLLITQAAKIAFPSLHPWVLILGNAKLRKASLSALQWLRCRHKDEHRRVQRPEVHSCGSSCMP
|
Putative taste receptor which may play a role in the perception of bitterness.
|
Q67ER8
|
A6TEI5
|
TRUB_KLEP7
|
tRNA-uridine isomerase
|
Klebsiella
|
MSRPRRRGRDVHGVLLLDKPQGASSNDVLQKVKRIYNANRAGHTGALDPLATGMLPICLGEATKFSQYLLDSDKRYRVIAKLGQRTDTSDADGQVVEERPLTFSDEQLAAALDSFRGETQQVPSMYSALKYQGKKLYEYARQGIEVPREARPITVYELLFIRREGDELELEIHCSKGTYIRTIIDDLGEKLGCGAHVIFLRRLAVSKYPVERMVTLEQLQALVDEAAAQDIPAAQLLDPLLMPMDSPASDYPLVNIPETSAVYFKNGNPVRQSGAPLNGLVRVMESESGKFLGMGEIDDEGRVAPRRLVVEYPA
|
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
|
A6TEI5
|
A5N8P8
|
THIG_CLOK5
|
Thiazole synthase
|
Clostridium
|
MDNLIIGGTEVKSRLFIGTGKYSSNSIIPRILKKSKSQVITIALRRVDITSKEENMLNYINKDCILLPNTSGARNAEEAIRLARIARAAGCGNWIKIEVISDNKYLLPDNYETIKATEVLAKEGFIVLPYMNPDLMDTKRLVNAGAAAVMPLGAPIGTNRGIATKEMIRIIIDEIATPIVVDAGIGKPSQAAEAMEMGADAVLVNTAIASAGNPVLMAEAFGLAVESGRKAFLAKLGQEKLMAEASSPLTGFLR
|
Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
|
A5N8P8
|
Q9CBG0
|
Y2020_MYCLE
|
Putative S-adenosyl-L-methionine-dependent methyltransferase ML2020
|
Mycobacterium
|
MAATPEFGSLRSDDDHWDIVSSVGYTALLVAGWRALHAVGPQPLVRDEYAKYFITASRDPYLMNLLANPGTSLNETAFPRLYGVQTRFFDDFFSSAGDTGIRQAVIVAAGLDSRAYRLKWPNGATVFEIDLPKVLEFKARVLAEQGAIPNAGRSEVAADLRADWPRALKAAGFDPQRSSAWSVEGLLPYLTNDAQSALFTRIGELCAPGSRIAVGALGSRLDRKQLAALEATHPGVNISGDVDFSALTYEPKTDSAQWLAAHGWAVEPVRNTLELQTSYGMTPPDVDVQMDSFMHSQYITATR
|
Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity.
|
Q9CBG0
|
Q8XK02
|
THIG_CLOPE
|
Thiazole synthase
|
Clostridium
|
MDKLIIGGIEIKNRLFVGSGKYPSNEIIKDVLEGSGSQVITLALRRVDLDNKEEDILQNIPKDVILLPNTSGATNAEEAIRIARIARAMGCGNWIKIEVISDSKYLLPDNEETIKATKVLADEGFIVLPYMCPDIYAGRRLIEAGAAAVMPLGAPIGSNRGLKTKELIQIMIDELDIPIIVDAGIGKPSQAMEAMEMGAAACLVNTAIASSEDPINMARAFKVAVEGGRLAYEAKMGRESKFGNASSPLTGFLD
|
Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
|
Q8XK02
|
A1WTL3
|
Y231_HALHL
|
Nucleoid-associated protein Hhal_0231
|
Halorhodospira
|
MKGGLGNIMKQAQKMQEDMQKAQEEIAAMEVSGEAGAGMVKVTMTGRNEVRKVEIDPSLFEDDREMVEDLVAAAVNDAVQKVQRESQERMSGMAEGMGLPPGMKLPF
|
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
|
A1WTL3
|
Q48BQ5
|
UBIA_PSE14
|
4-HB polyprenyltransferase
|
Pseudomonas
|
MYLSLLKSLNRLSPRAWDFIQLTRIDKPIGIYLLLWPTLWAVWIAGKGSPSLKTVFIFVVGVFLMRAAGCVINDFADRKVDGHVKRTEQRPLISGKVSSREALALFAVLVGLSFVLVLFTNATTIWLSFGGLALAACYPFMKRYTYYPQVVLGAAFSWGMPMAFTAETGDLPAAAWLLYIANLLWTVGYDTYYAMVDRDDDLKIGVKSTAVLFGDADRVIILTLQGLALGCLMLAGARFELGACFYIGLLAAAGCFAWEFWSTRQRERDACFKAFLHNHWAGLAIFLGIVADYAVR
|
Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate.
|
Q48BQ5
|
Q8S8X3
|
YCF3_ATRBE
|
Photosystem I assembly protein Ycf3
|
Atropa
|
MPRSRINGNFIDQTFSIVANILLRVIPTTSGEKEAFTYYRDGMSAQSEGNYAEALQNYYEAMRLEIDPYDRSYILYNIGLIHTSNGEHTKALEYYFRALERNPFLPQAFNNMAVICHYRGEQAIQQGDSEIAEAWFDQAAEYWKQAIALTPGNYIEAHNWLKITRRFE
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Essential for the assembly of the photosystem I (PSI) complex. May act as a chaperone-like factor to guide the assembly of the PSI subunits.
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Q8S8X3
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