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
|
|---|---|---|---|---|---|---|
P57880
|
TPX_PASMU
|
Thioredoxin-dependent peroxiredoxin
|
Pasteurella
|
MSKITLAGTEIEVSGVFPQVGDVVTDFTTVSAKLEDTTLANFAGKRKILNIFPSIDTGICATSVRKFNEQAAKLANTAVLCLSTDLPFAQARFCGAEGLENVFTVSTFRNKDVHKQLGVDIVEGPLAGLTARAVIVLDENNRVLHSELVPEIKQEPNYDAALAVL
|
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
|
P57880
|
A4XUW4
|
UVRC_PSEMY
|
Excinuclease ABC subunit C
|
Pseudomonas
|
MSVSFDSSAFLATCSGRPGVYRMFDADARLLYVGKAKNLKKRLSSYFRKTGQAPKTAALVARIAQVETTITANETEALLLEQTLIKEWRPPYNILLRDDKSYPYVFLSDGEFPRLGIHRGAKKAKGRYFGPYPSALAIRESLSLLQKTFLVRQCEDSYYRNRTRPCLQYQIKRCKGPCVGLVSPEEYAEDVRHSVMFLEGRSNALSEELSASMEKASMALEFERAAELRDQISMLRRVQDQQSMEGGSGDVDVVAVMLNPGGACVHLISVRGGRVLGSKNFFPQVAIEEEGGEVLMAFLAQYYLGNAERDLPSELIVNVQHEDFSTLIEAVESLRGRSLSISLRVRGTRARWQQLAVTNAEQALAARLANRQHLAERFEALATVLEMDEPPQRMECFDISHSSGEATVASCVVFGPEGPLKSDYRRFNIEGVTPGDDYAAMHQALTRRFSKIKDGEGKLPDVLLVDGGKGQLAMAREVLQELAVPDLILLGVAKGTTRKPGLEVLYLNDAEHEFTLPGNSPALHLIQQIRDESHRFAITGHRARRGKARRTSTLEEVAGIGPKRRRELLNHFGGLQELSRASAEEIAKAPGISKKLAELIYATLHSE
|
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.
|
A4XUW4
|
Q601T9
|
TMCAL_MESH2
|
tRNA(Met) cytidine acetate ligase
|
Mesomycoplasma
|
MAIAIIAEYNPFHNGHIYQLEYTKKNFPNDKIYIILSGNFTQRGEISLADFKTKSKIALKYGADFIIKLPFEYATQAAHIFAKGAIKIVNQHKIDKIIFGSESNDVENLYKLANLWNQNQEAYNAFLKYALKLGYSFPKASAFALEEISGQKIVFPNDILGFEYIKQIVANNYPIRAYTLKRSEEFSLKNPEPNIASATYLRQLVNENKSISRFSPMKFIHPVCSLANLYPEFQKIVRETSAENLAKIWLISEGIENLFKKHINEPNFEKFLNAVNSRRYTNSRIKRAMVYILFRIEDPSQFDEEKIQLDCWKNQGF
|
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.
|
Q601T9
|
Q5L6W5
|
YIDD_CHLAB
|
Putative membrane protein insertion efficiency factor
|
Chlamydia
|
MSFKQLLYNLPTHLCCGLIHLYRWTISPLLGSPCRFFPSCSQYALQALKHHKCIRGLWLTIKRIGKCGPWHPGGIDLVPMTTLEEALDVSQVTNDDDSGDSHA
|
Could be involved in insertion of integral membrane proteins into the membrane.
|
Q5L6W5
|
Q05938
|
TOXR_VIBPA
|
Cholera toxin homolog transcriptional activator
|
Vibrio
|
MTNIGTKFLLAQRFTFDPNSNSLADQQSGNEVVRLGSNESRILLMLAERPNEVLTRNELHEFVWREQGFEVDDSSLTQAISTLRKMLKDSTKSPEFVKTVPKRGYQLICTVERLSPLSSDSSSIEVEEPASDNNDASANEVETIVEPSLATTSDAIVEPEAPVVPEKAPVASAVNPWIPRVILFLALLLPICVLLFTNPAESQFRQIGEYQNVPVMTPVNHPQINNWLPSIEQCIERYVKHHAEDSLPVEVIATGGQNNQLILNYIHDSNHSYENVTLRIFAGQNDPTDICK
|
In the presence of ToxS, promotes the expression of the thermostable direct hemolysin 2. May be a global regulator.
|
Q05938
|
A4QKK3
|
YCF4_CAPBU
|
Photosystem I assembly protein Ycf4
|
Capsella
|
MSWRSESIWIEFITGSRKTSNFCWAFILFLGSLGFLLVGTSSYLGRNVISLFPSQQIIFFPQGIVMSFYGIAGLFISCYLWCTILWNVGSGYDLFDRKEGIVRIFRWGFPGKTRRIFLRFFMKDIQSIRIEVKEGVSARRVLYMEIRGQGAIPLIRTDENFTTREIEQKAAELAYFLRVPIEVF
|
Seems to be required for the assembly of the photosystem I complex.
|
A4QKK3
|
Q04FR4
|
TYSY_OENOB
|
Thymidylate synthase
|
Oenococcus
|
MSRNEEQYLNLARRILETGASKMDRTKTGTHSIFGAQMRFDLSEGFPLLTSKKVAFGRIKSELLWFLRGDNNIRFLLQHHNHIWDEWPFKKWVESNEYKGPDMTDFGLRTQKDPIFAEQYKEQKKIFVDRILNDDEFSKKFGTIGDVYGKLWRHWPDANDDGSVDQITRLINEIKVNPNSRRLILTAWDPETTPFATLPSCHVMSQFYVVDGKISLQMYQRSADYFLGVPFNIASYSLLLSMVAAQTGLEVGEFIHTIGDAHIYNNHVDQIKEQLSKPTHKLPTLKLNPDVKSIFDYEMSDIKLENYIHEDVIKAPIAV
|
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
|
Q04FR4
|
V9VGU0
|
VCL_PINKO
|
Vicilin-type seed storage protein
|
Pinus subgen. Strobus
|
MAFVSLLTILLAISSSSVALTEPVASMADQGVFPEQHGRGHHGVFPEEHGRGHHRGGREEEREENPYVFHSDRFRIRASSEAGEIRALPNFGEVSELLEGISRYRVTCIEMKPNTVMLPHYIDAKWILYVTGGRGYIAYVQQNELVKRKLEEGDVFGVPSGHTFYLVNNDDHNSLRIASLLRTESTMRGEYEPFYVAGGRNPETVYSAFSDDVLEAAFNTDVQKLEHIFGAHRRGVIFYANEEQIREMMRRGGFSAESTSASEQPKPFNLRNQKPDFENDNGRFTRAGPKDNPFLDSVDVTVGFGVLNPGTMTAPSHNTKATSIAIVMEGEGRIEMACPHLGQEHGWSSPRERGHQDINYERVRARLRTGTVYVVPAGHPITEIASTNGRLEILWFDINTSGNEREFLAGKNNVLQTLEKEVRHLSFNIPRGEEIEEVLQAQKDQVILRGPQRQRRDEPRSSS
|
Seed storage protein.
|
V9VGU0
|
A1WZH9
|
TSAC_HALHL
|
tRNA threonylcarbamoyladenosine biosynthesis protein TsaC
|
Halorhodospira
|
MNECPPGTRPFRVRHAAAELRQGGVVAYPTEAVWGLGCDPRNADAVARLLALKGRPERQGLILIAAESRQLARYLAPLPAEWAETIQASWPGPMTWVLPASTRAPRWVSGGRDTLAVRVTAHPVAAALCSAFGGALVSTSANPSARRPARSVAEVRRYFGTRIDALVPGRLGGLERPTPIRDGRSGAYLRR
|
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate.
|
A1WZH9
|
A7I4T7
|
TRPD_METB6
|
Anthranilate phosphoribosyltransferase
|
Methanoregula
|
MTMKEAIATVVEGRDLAPAQAAAVMNMMMDGQATPAQIGGFLTALRAKGETPEEIAAFARVMREHTVHVKPRVSGTLVDTCGTGGDGAQTFNISTAAAFVAAGAGITVVKHGNRSVSSRCGSADVLTALGVDISVDPGRQAGIVQETGIIFLFAPSHHPAMKHVMATRQDLGCRTVFNLLGPLANPAGAAAQVLGVYDQKLTGPMAEVLSLLGVSRAMVVFGSGLDEITVTGETSVTELANSRITNYIVTPEQFGFTRAAPGDLLGGDPEKNARIIRAILDGAPGPARDIVLMNAGAAIYVGGRAATLAEGIRHAAESIDSGKAAGKLAALVTATRGAS
|
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
|
A7I4T7
|
Q9ZRB1
|
TBB2_WHEAT
|
Beta-2-tubulin
|
Triticum
|
MREILHIQGGQCGNQIGAKFWEVVCDEHGIDPTGRYTGTSDLQLERVNVYYNEASCGRFVPRAVLMDLEPGTMDSVRTGPYGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGKMSTKEVDEQMINVQNKNSSYFVEWIPNNVKSSVCDIPPTGLSMASTFVGNSTSIQEMFRRVSEQFTSMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATSDEEGEYEDEDQEPEEDM
|
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.
|
Q9ZRB1
|
B9DM46
|
TRUA_STACT
|
tRNA-uridine isomerase I
|
Staphylococcus
|
MRILVKISYQGSNFLGFQIQQHGRTVQQQFEKILKRMHKRHVRIHPSSRTDRGVHAIEQYFHFDTELNIAPDKWQYAMNSALPDDIYVNEVSIVDDDFHCRYDCVGKRYRYKVYQGKHRDVFMSGLKTFYADSLDLEKMNEAAQQFIGTHDFTGFCSQKTEVESKERTLYQSEIIKTENGFDYIVTGSGFLYNMVRVLVAFLIEVGKGKRQPEEVPILLEAKDRKQVPFTAPAEGLYLEKIYLAPQELINDFGPDIKIHRKKSLEND
|
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
|
B9DM46
|
Q47HQ5
|
TRPB_DECAR
|
Tryptophan synthase beta chain
|
Dechloromonas
|
MSQYNFPDAKGHFGPYGGVFVAETLFGALDELKEAYAAAQADPAFRAEYEYELKHFVGRPSPIYHAKRWSEMLGGAQIYLKREDLNHTGAHKVNNCIGQAMLAKRMGKPRVIAETGAGQHGVATATVAARYGMECVVYMGSEDVKRQAANVYRMKLLGATVVPVESGSKTLKDALNEAMRDWVTNIHNTFYIIGTVAGPHPYPMLVRDFQKIIGEECLVQMPEMTGRQPDAVIACVGGGSNAMGIFYPYINVEGVRLIGVEAAGDGMETGRHSASLTAGVPGVLHGNRTYLLQDEDGQIIETHSVSAGLDYPGVGPEHAWLKDLGRAEYQPVTDSEALAAFHTLCRIEGIIPALESSHALAYAAKLAPTLAKDKILLVNLSGRGDKDMHTVAEKSGIVF
|
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
|
Q47HQ5
|
Q0HHA0
|
TIG_SHESM
|
PPIase
|
Shewanella
|
MQVSVEATQGLERRLTISVPAEQIEKLVKDSLQREAKRARIPGFRPGKVPVTVINKRYGAAIRQDITGEVMQRNFIEAIIAEKLNPAGAPTFVPGATDGEKFEFVATFEIYPEVELKGLDAIEVEQPKASVTDADVDSMIETLRKQHATFAAVEREAADGDKVKMNFVGSVDGVEFEGGKADDFELQLGSGRMIPGFEAGILGHKAGEEFVIDVTFPEEYHAENLKGKAAKFAITLTEVLAANLPEVNDEFAALFGISEGGLEALKTEIRKNMNRELEQALKANVKEQVINGLLANNDIELPKALIDGEVNVLRQQAMQRFGGQTANMPELPAELFTEQAARRVKIGLLLGEVIKTNELKAEDERVQALIASMASAYEDPSEVVAYYNSNKELMQNMRNVALEEQAVEALLKSAKVTEKEVAFEEFMNKATGRA
|
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
|
Q0HHA0
|
O95932
|
TGM3L_HUMAN
|
Transglutaminase-6
|
Homo
|
MAGIRVTKVDWQRSRNGAAHHTQEYPCPELVVRRGQSFSLTLELSRALDCEEILIFTMETGPRASEALHTKAVFQTSELERGEGWTAAREAQMEKTLTVSLASPPSAVIGRYLLSIRLSSHRKHSNRRLGEFVLLFNPWCAEDDVFLASEEERQEYVLSDSGIIFRGVEKHIRAQGWNYGQFEEDILNICLSILDRSPGHQNNPATDVSCRHNPIYVTRVISAMVNSNNDRGVVQGQWQGKYGGGTSPLHWRGSVAILQKWLKGRYKPVKYGQCWVFAGVLCTVLRCLGIATRVVSNFNSAHDTDQNLSVDKYVDSFGRTLEDLTEDSMWNFHVWNESWFARQDLGPSYNGWQVLDATPQEESEGVFRCGPASVTAIREGDVHLAHDGPFVFAEVNADYITWLWHEDESRERVYSNTKKIGRCISTKAVGSDSRVDITDLYKYPEGSRKERQVYSKAVNRLFGVEASGRRIWIRRAGGRCLWRDDLLEPATKPSIAGKFKVLEPPMLGHDLRLALCLANLTSRAQRVRVNLSGATILYTRKPVAEILHESHAVRLGPQEEKRIPITISYSKYKEDLTEDKKILLAAMCLVTKGEKLLVEKDITLEDFITIKVLGPAMVGVAVTVEVTVVNPLIERVKDCALMVEGSGLLQEQLSIDVPTLEPQERASVQFDITPSKSGPRQLQVDLVSPHFPDIKGFVIVHVATAK
|
Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins.
|
O95932
|
A2C0L6
|
YIDD_PROM1
|
Putative membrane protein insertion efficiency factor
|
Prochlorococcus
|
MLTKINKAIALVFVSLISFYQKWISPLFGPSCRFIPSCSAYGIEAVNKHGPWRGGWLTLKRLSKCHPFTPCGCDPVPEK
|
Could be involved in insertion of integral membrane proteins into the membrane.
|
A2C0L6
|
Q4A898
|
TMCAL_MESH7
|
tRNA(Met) cytidine acetate ligase
|
Mesomycoplasma
|
MAIAIIAEYNPFHNGHIYQLEYTKKNFPNDKIYIILSGNFTQRGEISLADFKTKSKIALKYGADFIIKLPFEYATQAAHIFAKGAIKIVNQHKIDKIIFGSESNDVENLYKLANLWNQNQEAYNAFLKYALKLGYSFPKASAFALEEISGQKIVFPNDILGFEYIKQIVANNYPIRAYTLKRSEEFSLKNPEPNIASATYLRQLVNENKSISRFSPMKFIHPVCSLPNLYPEFQKIVRETSAENLAKIWLISEGIENLFKKHINEPNFEKFLNAVNSRRYTNSRIKRAMVYILFRIEDPSQFDEEKIQLDCWKNQGF
|
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.
|
Q4A898
|
Q6CL17
|
VPS27_KLULA
|
Vacuolar protein sorting-associated protein 27
|
Kluyveromyces
|
MALPSMSVSEFDALIEQCTNEKIPNGEIDLSAALELSDMIRSRRLPPKDAMRCLKKRVLQTRNNQNLQFSVWRLVEVCMKNGGVPFLKEVCSREFMDCLEQVILAESTDYELEQFCSRLVGELYLAFKNDSQLSYVVKVYQKLVSRGIDMENLKPTENLNAMFDAKTPADWIDSDACMICSTQFTLLNRKHHCRSCGGVFCQLHSSKFIPLPDLGIFEPVRVCDNCFEDYDLKRKSSKGKKSKGKKRFTRSEDDDEDLRRAIELSLKENGRDADTFIPDTAKLEPLKKDPDEEDPDLKAAIEASLREHQQEEMRRKSQAKNMYNTSSPSVAPPIENNYDLSSNEEEDIHLFASLVERMKTQPPTAVLEDTQLQQLYQKVLGVRPKLNYALSDTVSKYNTVYEMNSKISDIMNMYDSMLEMQLRNISLSQQYAIPESGRNSYGYHQNMPQYDQPNSPQIIAQPQIHSPQQNERTILNYASPVSQHLSNGATTNTYQQGSALQNQQPAAPEPQPVSFEKPSTTSQLEGLILEEPSEPPYPDENTTIENPKIEQASERPYPDDHLKQENITSFDFPTVPLRKLSIHGSEQEVKEEPVQQEQLLIEL
|
Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB) and recruits ESCRT-I to the MVB outer membrane.
|
Q6CL17
|
B0S0L6
|
THIM_FINM2
|
4-methyl-5-beta-hydroxyethylthiazole kinase
|
Finegoldia
|
MDNLIQKMSEIYSDLHNSNNLIHCLTNAISINDMANAVLSIGQSPFMADNPREVEDVTRKSDSLLVNLGNITDYRIESIKKSVRIANENNIPITLDLVGVSASKLRLDLTLDILKNHTITCIKGNYSEIKSLFIKDLSTKGVDSQKLEVDDVINCCKNLHEKYDSIIVATGQTDIVCANEIYLLNNGDDRLSKITATGCVVGSLIACTLSVSQSIKACVLAISMMNISCEMVDKSVGLSSFKLGLYDNLSRIKWEQIKENIDAKKVES
|
Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
|
B0S0L6
|
P0C2E9
|
TACY_CLOPE
|
Thiol-activated cytolysin
|
Clostridium
|
MIRFKKTKLIASIAMALCLFSQPVISFSKDITDKNQSIDSGISSLSYNRNEVLASNGDKIESFVPKEGKKTGNKFIVVERQKRSLTTSPVDISIIDSVNDRTYPGALQLADKAFVENRPTILMVKRKPININIDLPGLKGENSIKVDDPTYGKVSGAIDELVSKWNEKYSSTHTLPARTQYSESMVYSKSQISSALNVNAKVLENSLGVDFNAVANNEKKVMILAYKQIFYTVSADLPKNPSDLFDDSVTFNDLKQKGVSNEAPPLMVSNVAYGRTIYVKLETTSSSKDVQAAFKALIKNTDIKNSQQYKDIYENSSFTAVVLGGDAQEHNKVVTKDFDEIRKVIKDNATFSTKNPAYPISYTSVFLKDNSVAAVHNKTDYIETTSTEYSKGKINLDHSGAYVAQFEVAWDEVSYDKEGNEVLTHKTWDGNYQDKTAHYSTVIPLEANARNIRIKARECTGLAWEWWRDVISEYDVPLTNNINVSIWGTTLYPGSSITYN
|
A cholesterol-dependent toxin that causes cytolysis by forming pores in cholesterol-containing host membranes. After binding to target membranes, the protein assembles into a pre-pore complex. A major conformational change leads to insertion in the host membrane and formation of an oligomeric pore complex. Cholesterol is required for binding to host cell membranes, membrane insertion and pore formation; cholesterol binding is mediated by a Thr-Leu pair in the C-terminus. Can be reversibly inactivated by oxidation.
|
P0C2E9
|
Q6D075
|
YQGF_PECAS
|
Putative pre-16S rRNA nuclease
|
Pectobacterium
|
MSNRTLLAFDFGTKSIGVAIGQEITGTARALTSFKAQEGIPDWQKVEKLLSEWQPDLVVVGLPLNMDGTEQPLTARARKFANRLHGRFGVAIELHDERLSTVEARADLFERGGFKALDKGSVDAASAVIILESWFEAQH
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
|
Q6D075
|
B7V362
|
THIC_PSEA8
|
Thiamine biosynthesis protein ThiC
|
Pseudomonas
|
MSATQKNNITRLEQLDRQSTQPFPNSRKVYLTGSRPDIRVPVREISLADTPTAFGGEKNPPVFVYDTSGPYTDPEVRIDLRKGLPDVRSRWIDERGDTEILPGLTSEFGQARLADASLDALRFAHVRTPRRAKPGANVSQMHYAKKGIITPEMEYIAIRENMKLQEARAAGLLDQQHPGHSFGANIPKEITPEFVREEVARGRAIIPANINHTELEPMIIGRNFLVKINGNIGNSALGSSIEEEVEKLTWGIRWGADTVMDLSTGKHIHETREWILRNSPVPIGTVPIYQALEKVNGVAEDLTWEIFRDTLIEQAEQGVDYFTIHAGVLLRYVPLTAKRVTGIVSRGGSIMAKWCLAHHQENFLYTHFEEICEIMKAYDVSFSLGDGLRPGSVADANDAAQFGELETLGELTKIAWKHDVQVMIEGPGHVPMQLIKENMDKQLECCDEAPFYTLGPLTTDIAPGYDHITSGIGAAMIGWFGCAMLCYVTPKEHLGLPNKDDVKTGIITYKIAAHAADLAKGHPGAQIRDNALSKARFEFRWEDQFNLGLDPDTARAFHDETLPKDSAKVAHFCSMCGPKFCSMKITQEVRDYAKENGLSDESKAIEAGFQEQAARFKDEGSVIYRQV
|
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.
|
B7V362
|
P40746
|
TGL_BACSU
|
Transglutaminase
|
Bacillus
|
MIIVSGQLLRPQDIENWQIDQDLNPLLKEMIETPVQFDYHSIAELMFELKLRMNIVAAAKTLHKSGAKFATFLKTYGNTTYWRVSPEGALELKYRMPPSKAIRDIAENGPFYAFECATAIVIIYYLALIDTIGEDKFNASFDRIILYDWHYEKLPIYTETGHHFFLGDCLYFKNPEFDPQKAQWRGENVILLGEDKYFAHGLGILNGKQIIDKLNSFRKKGALQSAYLLSQATRLDVPSLFRIVR
|
Probably plays a role in the assembly of the spore coat proteins by catalyzing epsilon-(gamma-glutamyl)lysine cross-links. In wild-type spores at 37 degrees Celsius, tgl mediates the cross-linking of GerQ in higher molecular mass forms, probably in cooperation with YabG.
|
P40746
|
B1YJJ2
|
THIM_EXIS2
|
4-methyl-5-beta-hydroxyethylthiazole kinase
|
Exiguobacterium
|
MLRRIHDKKPLIHHLTNTVTINDCANMTLALGGSPVMAEDLLEVEEMVGLADAVVINTGTINPDMRKAQLLAGKTANRLGKPVILDPVGAGATTLRTDFMKQLMEEITFTVIKGNASEIKTLLGQAARTKGVDVAEGESLDLQSVHAFASQTKQVIVVTGPVDFVTDGVRQHHLDVGTKRLGQVTGTGCMTASLIATFLGAGYGRFDAAVFGTYAMGKAGETAGNRPGIGSFRTGLFDAVSLMTEESLPEVQMNGQ
|
Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
|
B1YJJ2
|
Q53H54
|
TYW2_HUMAN
|
tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferase
|
Homo
|
MRENVVVSNMERESGKPVAVVAVVTEPWFTQRYREYLQRQKLFDTQHRVEKMPDGSVALPVLGETLPEQHLQELRNRVAPGSPCMLTQLPDPVPSKRAQGCSPAQKLCLEVSRWVEGRGVKWSAELEADLPRSWQRHGNLLLLSEDCFQAKQWKNLGPELWETVALALGVQRLAKRGRVSPDGTRTPAVTLLLGDHGWVEHVDNGIRYKFDVTQCMFSFGNITEKLRVASLSCAGEVLVDLYAGIGYFTLPFLVHAGAAFVHACEWNPHAVVALRNNLEINGVADRCQIHFGDNRKLKLSNIADRVILGLIPSSEEGWPIACQVLRQDAGGILHIHQNVESFPGKNLQALGVSKVEKEHWLYPQQITTNQWKNGATRDSRGKMLSPATKPEWQRWAESAETRIATLLQQVHGKPWKTQILHIQPVKSYAPHVDHIVLDLECCPCPSVG
|
S-adenosyl-L-methionine-dependent transferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the transfer of the alpha-amino-alpha-carboxypropyl (acp) group from S-adenosyl-L-methionine to the C-7 position of 4-demethylwyosine (imG-14) to produce wybutosine-86.
|
Q53H54
|
Q9XCW4
|
VIOA_ECOLX
|
dTDP-4-amino-4,6-dideoxy-D-glucose transaminase
|
Escherichia
|
MNDKTIPVTQPSLPELAEFMPYLEKIWKNKWLTNNGPFHQELEEKLCEFLGVQHISLFNNATIALITALQALRITGEVITTPYSFVATSHAILWNGLTPVFVDIENDGYNIDYRKIEQAITPKTSAILPVHCYSTPCEVEEIQKIADNYGLKVIYDAAHAFGVNFKGGKVYLTMVIYQFLVSMRRKSSINFEGGAIISPDAKTKLRIDRLKNFGIADELTVTAPGINGKMSEINAAFGLVQLKHIEGSISKRKIIDSLYRNLLKGTPGITIFPGNINTNSNYSYFPILIDDGFHMSRDQAYELLKKNNILSRKYFYPLISNMPMYRGLISASVDNLPIANSVADKVLCLPIYTDLNEEIVVKITKLLLGKM
|
Catalyzes the conversion of dTDP-4-dehydro-6-deoxy-D-glucose (dTDP-D-Glc4O) to dTDP-4-amino-4,6-dideoxy-D-glucose (dTDP-D-Qui4N).
|
Q9XCW4
|
Q815A2
|
TAGU_BACCR
|
Polyisoprenyl-teichoic acid--peptidoglycan teichoic acid transferase TagU
|
Bacillus cereus group
|
MKKKILFWILGIIGILIIGGGAYAYSIYSSVSKTLDEVHKPLKRDKDSKGTEEVKISKSEPVSILLLGVDERGNEKGRSDSLILITLNPKNNSMKTVSIPRDTYTEIVGKGKSDKINHAYAFGGVDMSVATVEKFLNVPINYYIEVNMAGFKDIVDAVGGVDVNNDLEFKQDKHHFAKGNIHLTGDEALSFTRMRYEDPRGDFGRQMRQRQVMQAVIKKGATFSSLTSYGDVLTAIQKNVKTNLTQDQMFDMQKNYKNCLENSEDIQIPGDGHKAADGIWYYYVPEAAKQDLTNKLRAHLEVTK
|
May catalyze the final step in cell wall teichoic acid biosynthesis, the transfer of the anionic cell wall polymers (APs) from their lipid-linked precursor to the cell wall peptidoglycan (PG).
|
Q815A2
|
Q15776
|
ZKSC8_HUMAN
|
Zinc finger protein 192
|
Homo
|
MAEESRKPSAPSPPDQTPEEDLVIVKVEEDHGWDQESSLHESNPLGQEVFRLRFRQLRYQETLGPREALIQLRALCHQWLRPDLNTKEQILELLVLEQFLTILPEELQTLVKEHQLENGEEVVTLLEDLERQIDILGRPVSARVHGHRVLWEEVVHSASAPEPPNTQLQSEATQHKSPVPQESQERAMSTSQSPTRSQKGSSGDQEMTATLLTAGFQTLEKIEDMAVSLIREEWLLDPSQKDLCRDNRPENFRNMFSLGGETRSENRELASKQVISTGIQPHGETAAKCNGDVIRGLEHEEARDLLGRLERQRGNPTQERRHKCDECGKSFAQSSGLVRHWRIHTGEKPYQCNVCGKAFSYRSALLSHQDIHNKVKRYHCKECGKAFSQNTGLILHQRIHTGEKPYQCNQCGKAFSQSAGLILHQRIHSGERPYECNECGKAFSHSSHLIGHQRIHTGEKPYECDECGKTFRRSSHLIGHQRSHTGEKPYKCNECGRAFSQKSGLIEHQRIHTGERPYKCKECGKAFNGNTGLIQHLRIHTGEKPYQCNECGKAFIQRSSLIRHQRIHSGEKSESISV
|
May be involved in transcriptional regulation.
|
Q15776
|
B9M422
|
UVRC_GEODF
|
Excinuclease ABC subunit C
|
Geotalea
|
MIEIDSIGHFPSSPGVYIMKDAEATVLYVGKARDLRKRIRSYFAASGDSRYQIRFLMARVTDIQFIVTDTEKEALILENTLIKKYRPKYNFNLRDDKTYFSLRMDMSSDFPRLSIIRKVTRDGARYFGPYSSASDARAVLKHLYKLFPLRHYPMETCRRRNRPCLFYQLKQCSAPCHGKISREDYMALAEGAALFLEGKNREILKIFRERMSAAAAAEKYEKAARFRDLIRSIEVTVEKQKVVAQGGDSDVIGFYREGEQLHIALLFLRGGTLTGSRNYSFSWEMDDHEGIASFLNEYYNQEVFIPSEIVLPIAIADPLPQEELLCELRGRRVSITVPQRGNKLELVRLAIKNAETAAAERKKAAESGEAILQTLKERLHLHKLPRRIECYDISNIQGQMAVGSKVAFVDGKADKAHYRRYRIKGVSQSDDFAMMREMFSRRFKPGTAPDDYPDLIIVDGGIGQLNVLTHVLGDLQITDVEAAGLAKSRVDREMGATEISRSDERVFLPNRKNPVVLRQNSAPLLLLARIRDEAHRFAVAYHKKLRGNKLLASQLEAIPGIGIKRRKELLRHFGSLKKISEATLEELRQVQGISATVAESLWKHLHENEKGDTNASPFVNFE
|
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.
|
B9M422
|
Q0TPH6
|
YQGF_CLOP1
|
Putative pre-16S rRNA nuclease
|
Clostridium
|
MRILGLDIGSKTIGVAVSDPLGWTAQGVTTIKRDCYTKDVEAVMKICKEYGVETIVAGMPKNMNGTIGPSGEMVKNLCEQIEKSFDGKIEFWDERLTTVAAHRAMLEADLSRAKRKKIVDKIAATYILQGYLDRISK
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
|
Q0TPH6
|
Q8CPZ0
|
UVRB_STAES
|
Excinuclease ABC subunit B
|
Staphylococcus
|
MVEHVPFKLKSEFEPQGDQPQAIQKIVDGVNERKRHQTLLGATGTGKTFTMSNVIKEVGKPTLIIAHNKTLAGQLYSEFKEFFPENRVEYFVSYYDYYQPEAYVPSTDTFIEKDASINDEIDQLRHSATSSLFERDDVIIIASVSCIYGLGNPEEYKNLVVSVRVGMEMERSELLRKLVDVQYSRNDIDFQRGTFRVRGDVVEIFPASREEMCIRVEFFGDEIDRIREVNYLTGEVIREREHFTIFPASHFVTREEKMKVAIERIEKELEERLKELRDENKLLEAQRLEQRTNYDLEMMREMGFCSGIENYSVHLTLRPLGSTPYTLLDYFGDDWLVMIDESHVTLPQIRGMYNGDRARKQVLIDHGFRLPSALDNRPLKFEEFEEKTKQLVYVSATPGPYELEHTDEMVEQIIRPTGLLDPKIDVRPTENQIDDLLSEIQDRVDKDERVLVTTLTKKMSEDLTTYMKEAGIKVNYLHSEIKTLERIEIIRDLRMGTYDAIVGINLLREGIDIPEVSLVVILDADKEGFLRSDRSLIQTIGRAARNDKGEVIMYADKITDSMQYAIDETQRRREIQIAHNKEHGITPKTINKKIHDVISATVESDETNQQQQTELPKKMTKKERQKTIENIEKEMKKAAKDLDFEKATELRDMLFELKAEG
|
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
|
Q8CPZ0
|
P0CI04
|
TX132_APHSP
|
Peptide 7-13.2
|
unclassified Aphonopelma
|
CLGENVPCDKDRPNCCSKYECLEPTGYGRCYASYYSYKKKTL
|
Inhibits voltage-gated calcium channels (Cav) in rat cerebellar granule cells.
|
P0CI04
|
A1W0N0
|
UVRC_CAMJJ
|
Excinuclease ABC subunit C
|
Campylobacter
|
MTKENLENELKTLPNSAGVYQYFNQEGKLLYVGKAKNLKNRVKSYFAFTPNLHANPRNSLRIQKMIEETVHLEFITTNSEADALILENSFIKQLHPKYNILLRDDKTYPYIYVNFEEEFPRFEITRKLVKKSKIKYFGPFFKGARELLDALYLYYPLKQKASCKSPCIFYQISRCLAPCDKRISKEKYLEILDEAMHALLNPSILIKNLEKQMLVLAQNENYEEAAKVRDQIVTIKDLEVKVEMDVAKLEDFEVFALAFEDSMLSTLRFVVQNGKIISANSKITPIKNDIQWDQNEIYKQLILENFSMDIPLLANVIYVYEEFEDRVLLEEILSQRFDKKISIKIPKIGEKRRICDLAFQNALLNIEKEQKNHDFTIQKELKFYFELENLPNDIEIFDNSHLQGVANVGAMVTYRINSWDKSKYRKFHLKHKNDYDQMREVLTRRALDFDKIPPPDLWLIDGGKVLLDLAKKIIVSSGANVDILAISKEKIDAKAHRAKGGAKDKIHSLKGEFSLSINDKKLQFLQKLRDEAHRFAISFHQNTKKKQDLKSSKLANLGLSSGVIQKLLAYYGNFESIYKADFKDLTMLVGRKAAQKIKEN
|
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.
|
A1W0N0
|
Q9GZ69
|
TPM_MIMNO
|
Allergen Chl n 1
|
Mimachlamys
|
MDAIKKKMQAMKVDRENAQDLAEQMEQKLKDTETAKAKLEEEFNELQKKLTATENNYDTVNEQLQEANTKLENSEKQITQLESDVGGLQRRLTLLEEDYERSEEKLNSTTEKLEEASKAADESERNRKVLEGRSNSYEERIDELEKQLETAKNVATDADHKFDEAARKLAITEVDLERAETRLEAADAKVLELEEELTVVGANIKTLQVQNDQASQREDSYEETIRDLTKSLKDAENRATEAERQVVKLQKEVDRLEDELLAEKERYKAISDDLDQTFAEIAGY
|
Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction.
|
Q9GZ69
|
C0MBD7
|
UVRB_STRE4
|
Excinuclease ABC subunit B
|
Streptococcus
|
MIDKRDFKAFKLVSKYAPSGDQPQAIETLVDNIEGGEKAQILLGATGTGKTYTMSQVISKVNKPTLVVAHNKTLAGQLYGEFKEFFPENAVEYFVSYYDYYQPEAYVPSSDTYIEKDSSVNDEIDKLRHSATSSLLERNDVIVVASVSCIYGLGSPKEYADSAVSLRPGQEISRDQLLNALVDIQFERNDIDFQRGRFRVRGDVVEVFPASRDEHAFRIEFFGDEIDRIREIESLTGKVLGDADHLVLFPATHFVTNDEHMEQSISKIQAELADQLKLFEAEGKLLEAQRLRQRTEYDIEMLREMGYTNGVENYSRHMDGRSAGEPPYTLLDFFPDDFLIMIDESHMTMGQIKGMYNGDKARKQMLVDYGFRLPSALDNRPLRREEFESHVHQIVYVSATPGDYEMEQTDTIVEQIIRPTGLLDPEVEVRPSMGQMDDLLGEINLRVERGERTFITTLTKKMAEDLTDYLKEMGVKVKYMHSDIKTLERTEIIRDLRLGVFDVLIGINLLREGIDVPEVSLVAILDADKEGFLRNERGLIQTIGRAARNADGHVIMYADRMTDSMQRAIDETARRRAIQMAYNEEHGIIPQTIKKDIRDLISISRAVEAKATEAETNYESMTRSERQEAIKQLQKNMQEAAELLDFELAAQLRDLILELKAMD
|
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
|
C0MBD7
|
Q944Q0
|
WNK8_ARATH
|
Protein kinase with no lysine 8
|
Arabidopsis
|
MASGSGFLGQISSMEEADFAEKDPSGRYIRYDDVLGRGAFKTVYKAFDEVDGIEVAWNLVSIEDVMQMPGQLERLYSEVHLLKALKHENIIKLFYSWVDEKNKTINMITELFTSGSLRVYRKKHRKVDPKAIKNWARQILKGLNYLHSQNPPVIHRDLKCDNIFVNGNTGEVKIGDLGLATVLQQPTARSVIGTPEFMAPELYEEEYNELVDIYSFGMCMLEMVTCEYPYNECRNQAQIYKKVTSNIKPQSLGKVDDPQVRQFIEKCLLPASSRPTALELSKDPFLARDGGKDSALLASSSTSSKYVRPPQLEHLPMDVDHNENKSVSSNEDYPWSQTIELQRIAENKEFRLRGERSDDVTASMVLRIADPSGKCRIVHFAFYLESDTATAIAEEMVEELHLTSQEVVVIADMIDDFIMQLLSDRTSSHHNQNSPRLTHEDHEAANQQTVNSKDEEAAGQSMKSDISADYYFPYSANDGNAAMEAGRDAESMSSYLDSCSMMSTIYNLSISDNDYPEDLKTELNLIESQFNQSFQDLLKLKEDAIENAKRKWITKKQKAVNIS
|
Regulates flowering time by modulating the photoperiod pathway. Phosphorylates the vacuolar ATPase subunit C (VATC) and RGS1 . Regulates EDM2 that, in turn, modulates development processes .
|
Q944Q0
|
Q57955
|
Y535_METJA
|
Uncharacterized protein MJ0535
|
Methanocaldococcus
|
MVSIMPKILYNPEVLGHKPKSYHVENPERVLTILNSLKSNGFDDIVLIEGKSTINEILEIHSRDYVYSIINLSKSFNYYDGDTYLCDRTLDAALTAFKLAKEAVKLALKDRDLYFALTRPPGHHAGISGRALGAMSNGFCIFNNIAGAARLAKNYMKKVIIIDFDVHHGNGTQEIFWNDNRVIHIDFHQRGIYPGTGDILDIGGEEAKGTKINLPFPAHSTDADYIFAWNEIVEPILNYFSPDTVLVSAGFDAFINDGLASMDLTETFYRFVGAKLSGYSVTAVLEGGYSIGLKYAPPAFLDGYVDAKDVLDNLEDYTVINSNEVKSMVKNVKKIIGEYLDIF
|
Putative deacetylase.
|
Q57955
|
P17794
|
VIRB4_AGRFC
|
Protein virB4
|
Agrobacterium tumefaciens complex
|
MLGASGTTERSGEVYLPYVGHVSDHIVLLEDGSIMTMAHVSGMAFELEDAEMRNARCRAFNTLLRNIADDHVSIYAHLVRHDDVPPSPARHFRSAFSASLSEAFEERVLSGKLLRNDHFLTLIVSPRAALGKVRRRFTKRYRQKENDLTAQTRNLEDLWHLVAGALEAYGLRRLGIREKQDVLFTEVGEALRLIMTGRFTPVPVVSGSLGASIYTDRVICGKRGLEIRTPKDSYVGSIYSFREYPATTRPGMLNVLLSLDFPLVLTQSFSFLTRSQAHSKLSLKSSQMLSSGDKAVTQISKLSEAEDALASNEFVLGAHHVSLCIYANDLNNLADRGARARTRLADAGAVVVQEGIGMEAAYWSQLPGNYKWRTRPGAITSRNFAGLVSFENFPEGSGSGHWGNAIARFRTNGGTPFDYIPHEHDVGMTAIFGPIGRGKTTLMTFILAMLEQSMVDRAGAVVLFDKDRGSELLVRATGGTYLALRRGAPSGLAPLRGLENTAASHDFLREWIVALIESDGRGGISPEENRRLVRGIHRQLSFDPHMRSIAGLREFLLHGPAEGAGARLQRWCRGNALGWAFDGELDEVKLDPSITGFDMTHLLEYEEVCAAAAAYLLHRIGAMVDGRRFVMSCDEFRAYLLNPKFAAVVDKFLLTVRKNNGMLILATQQPEHVLESQLGASLVAQCMTKIFYPSPTADRSAYIDGLKCTEKEFQAIREDMAVGSRKFLLKRESGSVVCEFDLREMREYVAVLSGRANTVRFADQLRKVQGDNPSAWLSEFMARYHEAKD
|
A possible function of virB4 might be to provide the energy, via hydrolysis of ATP, for translocation of virulence proteins of the transfer of a T-DNA-protein complex across the agrobacterium membrane.
|
P17794
|
O13267
|
WNT5A_PLEWA
|
Protein Wnt-5a
|
Pleurodeles
|
MASRYLTLAAALLASFLQVDIEANSWWSLAMNPVQIPEAYIVGAQPLCSQLAGLSPGQKKLCQLYQDHMQYIGEGAKTGIKECQYQFRHRRWNCSTVDNISVFGRVMQIGSRETAFTYSISAAGVVNAVSRACRAGELSTCGCSRARRPKDLQRDWLWGGCGDNLDYGYRFAKEFVDAREREKIHQKGSYESSRTLMNLHNNEAGRRTVYNLADVACKCHGVSGSCSLKTCWLQLADFRKVGDFLKEKYDSAASMKLNSRGKLVQVNSRFNPPTTNDLVYVDPSPDYCVRNESTGSMGTQGRLCNKTSEGMDGCELMCCGRGYDQFKTVQTERCHCKFHWCCYVKCKKCTEIVDQFVCK
|
Ligand for members of the frizzled family of seven transmembrane receptors. Can activate or inhibit canonical Wnt signaling, depending on receptor context. Required during embryogenesis for extension of the primary anterior-posterior axis.
|
O13267
|
Q65P74
|
TRUA_BACLD
|
tRNA-uridine isomerase I
|
Bacillus
|
MRMKCTISYDGHLFYGYQVQPGQRTIQDELEKALQTLHKAKERIPVVSSGRTDSGVHAVGQTIHFDSPLSIPEAKWPYALNALLPDDISVRKAEAVNDQFHARFSAKRKEYRYMIYRGRHPDVFKRYYAYHVPYDLDMEKVKEASRYLVGTHDFTSFCATKTEVKDKVRTVHELEWSDTGDGLQMRIVGSGFLYNMVRIIAGTLLDVGTGKFSPGDIEKMILAKNRDAAGRTAPAHGLYLWRVIYDN
|
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
|
Q65P74
|
Q9DBS2
|
TPRGL_MOUSE
|
Protein FAM79A
|
Mus
|
MLQLRDTVDSAGTSPTAVLAAGEDAGAGRPGAGTPLRQTLWPLNVHDPTRRARVKEYFVFRPGTIEQAVEEIRAVVRPVEDGEIQGVWLLTEVDHWNNEKERLVLVTDQSLLICKYDFISLQCQQVVRVALSAVDTISCGEFQFPPKSLNKREGFGVRIQWDKQSRPSFINRWNPWSTNMPYATFIEHPMAGMDEKTASLCHLESFKALLIQAVKKAQKESPLPGQANTVLVLERPLLIETYVGLMSFINNEAKLGYSMTRGKIGF
|
Presynaptic protein involved in the synaptic transmission tuning. Regulates synaptic release probability by decreasing the calcium sensitivity of release.
|
Q9DBS2
|
Q40289
|
UFOG7_MANES
|
UDP-glucose flavonoid 3-O-glucosyltransferase 7
|
Manihot
|
TLNLIPGMSKIQIRDLPEGVLFGNLESLFSQMLHNMGRMLPRAAAVLMNSFEELDPTIVSDLNSKFNNILCIGPFNLVSPPPPVPDTYGCMAWLDKQKPASVAYISFGSVATPPPHELVALAEALEASKVPFLWSLKDHSKVHLPNGFLDRTKSHGIVLSWAPQVEILEHAALGVFVTHCGWNSILESIVGGVPMICRPFFGDQRLNGRMVEDVWEIGLLMDGGVLTKNGAIDGLNQILLQGKGKKMRENIKRLKELAKGATEPKGSSSKSFTELANLVRSRGSYEN
|
In the presence of other necessary color factors, this glycosylation reaction allows the accumulation of anthocyanin pigments.
|
Q40289
|
A6WM46
|
TOLB_SHEB8
|
Tol-Pal system protein TolB
|
Shewanella
|
MRILAKWLALAVLLCTTPAKAALDIVITEGVDAARPIAVMPFVWQGPGAAPQAIADVVMSDLVRSGTFKPLDELGLPQRNIGTVAQFQANSWSSVGAEALVLGTVKPYGTDQYLVSFDLIDLVKAQNQALKGPVSATEFLMDSRQTVISAAQFRQYGHRISDIVYEKLTGIRGAFLTRISYVVVNHTQKAPYQLMVADYDGVNEQMLLRSPEPLMSPTWSPDGRRLAYVSFENKKAEIFVQDLYTQVRTKVSSFPGINGAPAFSPDGKSLAITLSKDGQPEIYIIDIATKAIKRITNHYAIDTEPSWYPDGKSLIFTSERGGRPQIYRVELSSGKVSRETFEGEWNLGGSITPDGRSMIFVNRTNGKFNIARMDLSTRFMQVLTSTRLDESPSVAPNGTMVIYGTTYQGKQVLAAVSTDGRFKARLPAGQGEVKSPSWSPFL
|
Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
|
A6WM46
|
A4Y3A9
|
Y712_SHEPC
|
Nucleotide-binding protein Sputcn32_0712
|
Shewanella
|
MKLVIVSGRSGSGKSVALRVLEDLGYYCVDNLPLPLIGSLLEQLKGSNDLVAISVDVRNMPEQDKVLVQQLSNLPAGTEITSFFLNSSDKVLLKRYSETRRLHPLSKSRVSLQEAIKLEGKLLEPMSKLVDHYIDTSNLNIYDLSDQVRQILLGSVDKELVIYFESFGFKNGMPTEADFMFDVRFLPNPHWELALRPLTGLDEPVAEFLNRQPLVNKFIWQIENLLETWLPHLERNNRSYLTIAIGCTGGQHRSVYVAEQLAKRFSNGKHKVNVRHRELDNAKA
|
Displays ATPase and GTPase activities.
|
A4Y3A9
|
B0M1H3
|
ZIP4L_ARATH
|
Protein ZIP4 homolog
|
Arabidopsis
|
MRIAEITTPDLRLHHRETDSHTHHPLLSEIELLIQQSEAISKDQPLPQSLPISLRQFLTRLSQLAPFPDNSFKLTIWKLSFRLWNACVDLANAASLQSSLTSAENIANLRHVAADMLFLAKDVTGVPSPTIKSSLFYYKTGLVYHSLKKFDLASDCFERATEIVSKIDIAKISDAGEKKLFLDLNLARSRTAWEISDRNLAVTLLNRAKNLLFGSPDHYKSLSNQFLAFGKSSLSRGDDDCSLNDALRLMNEALDLCEKGLGTAKTREDTTEFTAMRIKTLRFISAVHLQKGEFENVIKCVKVLRNGGNGSDGADQHASLPVLAMKAWLGLGRHSEAEKELRGMVGNNDIPEAVWVSAVEAYFEVVGTAGAETAKGVFLGLLGRCHVSAKAALRVAHRVLGESRGGDNGSRIRANVVAQLVSDERVVALFASEAVTKERKAIHSVLWNSASDHFRAKDYETSAEMFEKSMLYIPHDIENRVFRAKGFRVLCLCYLGLSQLDRALEYIEEAEKLEPNIACSFLKFKIYLQKKEHSCAIGQIDAMTSCLDFSPDYLSLSAHEAISCQALPVAVASLSKFLSFYISGKKMPTTEVVVFRTLVTILTQDIGSETEALNFMLQAQSRASKLGTECFFGLGETGKREQNWFAATCWNLGSRCGKEKKYELCGEFLRLASEFYGYIDTDESGEDKLMICRSIILSVTAMIALEKQTKSALTETQVKLAAELLVRAGKIMSSSLSDGKDCIMEPELIFMYTLLAYDIHGRLNNSAFQLLVVKTFAGSKSCHYNYLLQLGIFASQSPQSNPDVSTFALNECLSALIASASPEYPTIALIIRKLISIASVHKGDTDDEEAILKMYKQAYRIMVGLKEGEYPTEEGKWLAMTAWNRAALPVRLGQFETAKKWLSIGLEIADKVTGMDTYKACMQDYLAGFQTKVSSA
|
Required for meiotic chromosome segregation. It is involved in interference-sensitive crossovers (class I meiotic crossover) formation, in both male and female meiosis. Is specific to recombination events resulting in interference-sensitive crossovers (class I meiotic crossover). Not required for synapsis completion.
|
B0M1H3
|
A1JJ98
|
TYPH_YERE8
|
TdRPase
|
Yersinia
|
MFLAQEIIRKKRDGQALSEEEIRFFINGIRDNVVSEGQIAALAMTIYFHDMSMPERVALTMAMRDSGTVLNWKSLNLNGPMVDKHSTGGVGDVTSLMLGPMVAACGGYVPMISGRGLGHTGGTLDKLEAIPGFDIFPDDSAFRKIIQDVGVAIIGQTSSLAPADKRFYATRDITATVDSIPLITASILAKKLAEGLDALVMDVKVGSGAFMPTYQLSEDLAKAIVGVANGAGCKTTALLTDMNQVLASSAGNAVEVREAVRFLTGEYRNPRLLEVTMALCVEMLLSGGLAQNDADARAKLQAVLDNGKAAEIFGRMVAAQKGPSDFVERYDSYLPAAMLSKPVFAERSGIITAMDTRALGMAVVSLGGGRRRATDPIDYSVGLTEMARLGASVDGQQPLAVIHANNEDDWQQAADAVRAAITLGQKAAEETPVVYRRITE
|
The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis.
|
A1JJ98
|
Q868G6
|
TACHY_APIME
|
Tachykinin-related peptide 7
|
Apis
|
MIIHSIFLLMVSITLVIAEESDNVLFDKRAPTGHQEMQGKQNSASLNSENFGIFKRALMGFQGVRGKKNSIINDVKNELFPEDINKRAPMGFQGMRGKKASFDDEYYKRAPMGFQGMRGKKSLEEILDEIKKKTTRFQDSRSKDVYLIDYPEDYGKRVLSMDGYQNILDKKDELLGEWEKRAPMGFYGTRGKKIILDALEELDKRGVMDFQIGLQRKKDTTFDDYLDYAINPFDYEKRSTDFQDVESGSESFKRARMGFHGMRGKRDAAGIYGSNSSTVGTIFGYQDMRNRGNNFPVYQVEKRSPFRYLGARGKKNPRWEFRGKFVGVRGKKSSLQTVF
|
Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles. Associated with sex-specific or age/division of labor-selective behavior and/or physiology of honeybees.
|
Q868G6
|
B0TT74
|
UREG_SHEHH
|
Urease accessory protein UreG
|
Shewanella
|
MTELEYKQPLRIGVGGPVGSGKTALLEVLCKALRNKYQIAVVTNDIYTQEDAKILTRAEALDADRIIGVETGGCPHTAIREDASMNLAAVEELAKRHKNLDVVFVESGGDNLSATFSPELADLTIYVIDVAEGEKIPRKGGPGITRSDLLIINKIDLAPYVGASLVVMDQDTKRMRPEKPYIFTNMKTGKGVPEILTFIETAGMLNI
|
Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG.
|
B0TT74
|
P54402
|
TBG_EUPAE
|
Gamma-tubulin
|
Euplotes
|
MPREIITCQVGQCGNQIGMEFWKQLCMEHGINPEGILEDFAVNGEDRKDVFFYQADDEHYVPRAVLIDLEPRVINCIQKSTYSSLYNPENIYIAKHGGGAGNNWGRGYTDAEKVQDEILEMIDREADGSDSLEGFVLTHSIAGGTGSGFGSYLLERINDHYPKKLIQTYSVFPIENDVVVQPYNCLLSIKRLTLNADCVVVLDNNALTSIAVDRLKILQPTFSQINSIVSTVMAASTTTLRYPGYMNNDMVGLIASLVPTPRCHFLMTGYTPLSLDQKYTSVRKTTFLDVMRRLLQTKNIMVTGAVKKGAYMSILNVIQGDVDPTQVHKSLQRIKERKLANFIPWGPASIQVALAKKSPYIDSGHKVSGLMLANHTGIRSIFKVLYDQYRTFRKRDAYMNIFKQTKIFEDNLDEFDSSDEVVKNLIDEYAAAEKMDYINWGNDDDDMQFDPREPPKFSNIQ
|
Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome, suggesting that it is involved in the minus-end nucleation of microtubule assembly.
|
P54402
|
P33044
|
THHR_HORVU
|
Antifungal protein R
|
Hordeum
|
ATITVVNRCSYTVWPGALPGGGVRLDPGQRWALNMPAGTAGAAV
|
Has antifungal activity. Inhibits the growth of Trichoderma viridae and Candida albicans.
|
P33044
|
Q6NZL6
|
TONSL_MOUSE
|
Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor-like 2
|
Mus
|
MTLEQELRQLSKAKTRAQRNGQLREEAAYCHQLGELLASHGRFKDALEEHQQELHLLESVQDTLGCAVAHRKIGERLAEMENYSAALKHQHLYLDLAGSLSNHTELQRAWATIGRTHLDIYDHCQSRDSLLQAQAAFEKSLAIVDEKLEGMLTQRELSEMRTRLYLNLGLTCESLQQTALCNNYFKKSIFLAEQNHLYEDLFRARYNLGAIHWRGGQHSQAMRCLEGARECARAMKMRFMESECCVLVSQVLQDLGDFLAAKRALKKAYRLGSQKPNQRVTVCQSLKYVLAVIQLQQQLEEAEGNDLQGAMAICEQLGDLFSKAGDFPKAAEAYQKQLHLAELLNRPDLELAVIHVSLATTLGDMKDHRKAVHHYEEELRLRKGNALEEAKTWFNIALSREEAGDAYELLAPCFQKAFCCAQQAQRFQLQRQILQHLYTVQLKLQPQEARDTEIRLQELSMAKDTEEEEEEEEEEEEEASEAPETSELELSESEDDADGLSQQLEEDEELQGCVGRRKVNKWNRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCDGITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLETLQQWVKLYFRDLDLETRQKAATMEERLQMASSGQASRSSPALQTIPSNHLFDPETSPPSSPCPEPSSYTPRPPEASPAPAKVFLEETVSAVSRPRKTRHRPTSSSSSSEDEDNPSPCRPSQKRLRHTTQQGEVKIPDPPKSRETATSSACRAAYQAAIRGVGSAQSRRLVPSLPRGSEEVPAPKTALIPEEEYLAGEWLEVDTPLTRSGRPSTSVSDYERCPARPRTRVKQSRLTSLDGWCARTQAGDGSLNAEPAENPSVPRTSGPNKENYAAGQPLLLVQPPPIRVRVQIQDNLFLIPVPQSDIRPVAWLTEQAAQRYFQTCGLLPRLTLRKDGALLAPQDPIPDVLQSNDEVLAEVTSWDLPPLKDRYRRACLSLGQGEHQQVLHAMDHQSSSPSFSACSLALCQAQLTPLLRALKLHTALRELRLAGNRLGDACATELLATLGTTPNLVLLDLSSNHLGQEGLRQLVEGSSGQAALQNLEELDLSMNPLGDGCGQALASLLRACPMLSTLRLQACGFSSSFFLSHQAALGGAFQDAVHLKTLSLSYNLLGAPALARVLQTLPACTLKRLDLSSVAASKSNSGIIEPVIKYLTKEGCALAHLTLSANCLGDKAVRELSRCLPCCPSLTSLDLSANPEVSCASLEELLSALQERSQGLSFLGLSGCSIQGPLNSDLWDKIFVQLQELQLCTKDLSTKDRDSVCQRLPEGACTMDQSSKLFFKCL
|
Component of the MMS22L-TONSL complex, a complex that promotes homologous recombination-mediated repair of double-strand breaks (DSBs) at stalled or collapsed replication forks. The MMS22L-TONSL complex is required to maintain genome integrity during DNA replication. It mediates the assembly of RAD51 filaments on single-stranded DNA (ssDNA): the MMS22L-TONSL complex is recruited to DSBs following histone replacement by histone chaperones and eviction of the replication protein A complex (RPA/RP-A) from DSBs. Following recruitment to DSBs, the TONSL-MMS22L complex promotes recruitment of RAD51 filaments and subsequent homologous recombination. Within the complex, TONSL acts as histone reader, which recognizes and binds newly synthesized histones following their replacement by histone chaperones. Specifically binds histone H4 lacking methylation at 'Lys-20' (H4K20me0) and histone H3.1.
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Q6NZL6
|
B4G535
|
TOTZ_DROPE
|
Protein Turandot Z
|
Sophophora
|
MSRLIHLSFVLALLACLTGTISANPIDDDRDRLNQLLSNPEPADDAELLRNTQEAIALYKKHARRTLPGHQVELDLDRDIRAFETENLTVDGLPIQGGVWDLIKKGADKVPDEVKDQAKELAKTTAKALFNKLTEYLKKKISGEDAAKKDT
|
A humoral factor that may play a role in stress tolerance.
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B4G535
|
Q0VTA7
|
UBIA_ALCBS
|
4-HB polyprenyltransferase
|
Alcanivorax
|
MFAFVEQRYPTLWPYIQLMRLDRPIGTLLLLWPTLWAVWIAGAGTPSLTVIVVFFLGVVIMRAAGCVINDFADRNFDGDVERTQGRPLATGALSAKQALALFGGLGLLAFGLVLFLNELTFWLSFGGLGLAVLYPFTKRFTFMPQLFLGAAFSWAIPMAFAAETGEVPEIAWLLYVANVLWTVAYDTEYAMCDREDDLKLGIKSTAILFGDADRLMIAILQALTLLALIMVGHRLGFSWPWYAGLVGMSLSFAFQHSLIRYRERWPSFHAFLNNHWAGACVFIGLYFQYF
|
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.
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Q0VTA7
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Q0VMA0
|
TATA_ALCBS
|
Sec-independent protein translocase protein TatA
|
Alcanivorax
|
MFSGISIWQLLILLAIVVLLFGTKKLRNIGGDLGGAVKGFKSAMKDGEDEQDHKRLADDDQPQNKQDAEQKAEQEKDKA
|
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.
|
Q0VMA0
|
Q9RPY1
|
VIRB4_BRUSU
|
Type IV secretion system protein virB4
|
Brucella
|
MGAQSKYAQQLNNERSLAPFIPFRSQVGPTTVITRDGDFVRTWRIAGLAFETQDKEELLIRKDQLNTLFRAIASNNVALWSHNVRRRTWDHLKSFFSNPFCDALDKKYYGSFSGYRMMSNELYLTVIYRPVPAKISRLFNVAVHRSHAEILQEQQLAIRKLDEIGNQIETSLRRYGGDDGRGIEVLSTYEDKHGALCSQQLEFYNFLLSGEWQKVRVPSCPLDEYLGTGWVYAGTETIEIRTANATRYARGIDFKDYASHTEPGILNGLMYSDYEYVITQSFSFMTKRDGKEFLTRQKQRLQNTEDGSASQIMEMDIAIDQLGRGDFVMGEYHYSLLVFAEDMETVRHNTSHAMNILQDNGFLATVIATATDAAFYAQLPCNWRYRPRVAGLTSLNFAGLSCFHNFRAGKRDGNPWGQALTLLKTPSGQPAYLNFHYSKGDEDNFDKKLLGNTRIIGQSGAGKTVLMNFCLAQAQKYLHNAPMGMCNVFFDKDQGAKGTILAIGGKYLAIRNGEPTGFNPFQMEPTAGNILFLEKLVQVLVSRDGQHVTTTDESRISHAIRTVMRMRPELRRLSTVLQNVTEGSDRQDRENSVAKRLAKWCFDDGTGKRGTFWWVLDCPQDQIDFNTHSNYGFDGTDFLDNADVRTPISMYLLHRMELAIDGRRFIYWMDEAWKWVDDEAFSEFANNKQLTIRKQNGLGVFATQMPSSLLNSKVASALVQQVATEIYLPNPKADYHEYTDGFKVTNEEFDIIRSMSEESRMFLVKQGHHSMICRLELNGFDDELAILSGSSDNNELLDQVIAEVGDDPSVWLPVFQERRKARIASSKSTGR
|
The VirB system could be required for the establishment of the replication niche in the host.
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Q9RPY1
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Q08975
|
THI21_YEAST
|
Hydroxymethylpyrimidine phosphate kinase
|
Saccharomyces
|
MTYSTVNINTPPPYLALASNEKLPTVLSIAGTDPSGGAGVEADVKTITAHRCYAMTCITALNAQTPVKVYSINNTPKEVVSQILDANLQDMKCDVIKTGMLTTAAIEVLHEKLLQLGENRPKLVVDPVLVATSGSSLAGKDIASLITEKIAPFADILTPNIPECFKLLGEDREISKLRDIFEVAKDLAKITKCSNILVKGGHIPWNDEEGKYITDVLYLGAEQRFITFKGNFVNTTHTHGTGCTLASAIASNLARGYSLPQSVYGGIEYVQNAVAIGCDVTKETVKDNGPINHVYAIEIPLEKMLSDECFTASDAVHKKPVKSSLNKIPGGSFYKYLINHPKVKPHWDSYVNHDFVRKVADGSLEPKKFQFFIEQDYLYLVNYARISCIAGSKSPCLEDLEKELVIVECVRNGLCQHERRLREEFGIKDPDYLQKIQRGPALRAYCRYFNDVSRRGNWQELVIALNPCLMGYVHALTKIKDEVTAAEGSVYREWCETYSSSWCHEAMLEGEKLLNHILETYPPEKLDTLVTIYAEVCELEANFWTAALEYE
|
Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and also probably that of HMP to HMP-P.
|
Q08975
|
Q2SRU7
|
TRMD_MYCCT
|
tRNA [GM37] methyltransferase
|
Mycoplasma
|
MKFSIITLFPKIINSYIEESIIKRAINKQAIQIEIIDLRNFSTLNHNQVDDYQYGGGSGMVLMIEPLIKAIESVKTTKSIVLLTTPQGKTLNQSIVKTYSNNYEHIIIVCGHYEGYDERVLDYIDDEISIGDYVITGGELASLILVDSISRLLPNVIKQESYENESFENNLLDHPVYTKPYEFRNKKVPDVLLSGHHQNIKKWREEQQVIKTLKKRPDLIDITKLNKHQLEIYKKMKGEQ
|
Specifically methylates guanosine-37 in various tRNAs.
|
Q2SRU7
|
A3MV36
|
TBP_PYRCJ
|
TATA-box factor
|
Pyrobaculum
|
MSSKGPSYRIENIVATVNLGVELDLESLAERLPMAEYNPDQFPGLILRLTKPRISALIFRTGKMVCTGAKNEEDLKNAVRALVKLLNDHGAEVPFDPEVQIQNIVASGNLHAEVDLEQAVFMLENAMYEPEQFPGLIYRMSSPRVVILIFGSGKIVCTGAKSEKDVATAVQKLYNQLKELGVLYIEEGGGEEEEEEEEM
|
General factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Binds specifically to the TATA box promoter element which lies close to the position of transcription initiation.
|
A3MV36
|
Q8CQ77
|
TARI_STAES
|
Ribitol-5-phosphate cytidylyltransferase
|
Staphylococcus
|
MIYAGILAGGIGSRMGNVPLPKQFLSLQGKPIIIHTVEKFLMYKDFDEIIIATPQKWINYMLDLLNNYQLDDKKIKVIQGGDDRNHSIMNIIESIEQHKKLNDEDIIVTHDAVRPFLTNRIIRENVEYASQYGAVDTVVNAVDTIISSNDAQFISGIPIRSEMYQGQTPQTFKIKELKDSYLSLTQSQKEILTDACKILVELGKPVKLVKGELFNIKITTPYDLKVANSIITGAVDND
|
Catalyzes the transfer of the cytidylyl group of CTP to D-ribitol 5-phosphate.
|
Q8CQ77
|
B0TPX8
|
TOLB_SHEHH
|
Tol-Pal system protein TolB
|
Shewanella
|
MKIFGKWLLVTLLICSMPVKAALDIVITEGIDAARPIAVIPFVWQGTGPMPSQISDVVMSDLARSGTFSPADELSLPQRGISTLAQFNASAWMTQPAEAVVMGSIKPYGGDKYLVSFELIDLVKAQLQPDSQSAQDLVIDSRETIITAAQFRQYGHRISDVVYEKLTGIRGAFLTRIAYVVVNHGEKSPYKLMISDYDGYNEQMLLRSPEPLMSPSWSPDGQRLAYVSFENRKAEIYVQNIYTQQRTNVTSFDGINGAPVFSPDGKKLAVTLSKDGQPEVYVVDIATKAIKRVTNHYAIDTEPSWFPDGKSLLITSERGGRPQLYRVFLDSGKISRLTFEGEWNLGGSIAPDGRSIIFVNRTNGKFNIARMDLETRFMQVLTSTRLDESPSVAPNGTMVIYGTTYQGKQVLAAVSMDGRFKARLPVGQGEVKSPSWSPFL
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Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
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B0TPX8
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Q2SQW8
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TSAC_HAHCH
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tRNA threonylcarbamoyladenosine biosynthesis protein TsaC
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Hahella
|
MSAWFIQKAVSVLSRGGVLAYPTEAVWGLGCDPSCEDAVNRILQLKRRPWRKGLILVSGQIEHFSQLLDRLPQQQKDQILATWPGPVTWVVPDPGVYAPLVRGAHDAIAIRVTAHPLVVELTKAFGGPIVSTSANPATREPARTLFDCRRYFKSGVDHYLPGKLSGLSKPSQIRDAATGAILRQ
|
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate.
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Q2SQW8
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Q0BPX7
|
UVRC_GRABC
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Excinuclease ABC subunit C
|
Granulibacter
|
MTMPDAPANPPKEADNPSLPIVEAPPGKGVTVIEAMLKLLPDRPGVYRMLDGQGEALYVGKARSLKKRVASYTQIHRLPERLRRMVSETVSMEIVTTHTEAEALLLEANLIKRLKPRFNIVLRDDKSYPWLMLTEDHAFPQIMKHRGAQTRKAASYWGPFASAWAVNQTVTAMQRIFLLRSCSDSVFANRSRPCLLFQIRRCSAPCVDRISQEDYAELVDQARAFLSGRGTEIQRDLARQMEQAAEALEFERAAAIRDRIRGLTHVQGTAVVNPASIGNADVIAVWQDAGQSCVQVFFIRGGHNNGNRAFYPAHTSAETAQDVLGAFIAQFYDDKPPPPLLLLNHTIAEQELVSEALSLKAGRRVELHVPVRGEKRAVVAHAETNAREALERKLAESAGQNRLLDGVAELFDLPTRPNRIEIYDNSHIMGTNPYGVMVVAGPEGWNKSAYRKFSIRGPITPGDDFAMMREMLERRFSRGLKERAEGPEGEANWPDLVLIDGGAGQLSAVRGILDEIGVTDVKLVAIAKGPDRDAGREWFHTEGQAPFQLPPRDPVLYYLQRLRDEAHRFAITTHRAGRSKTLVRSELDDIDGIGAARKRALLNHFGSARGVKQAGLAALEATPGISKETARRIYAHFHPGARAD
|
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.
|
Q0BPX7
|
Q9LKI8
|
TBB_THAWE
|
Beta-tubulin
|
Conticribra
|
MREIVHIQGGQCGNQIGAKFWEVMSDEHGVDPTGTYHGDSDLQLERINVYFNEATGGRYVPRAILMDLEPGTMDSVRAGPFGQLFRPDNFVFGQTGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCMQGFQLTHSMGGGTGAGMGTLLISKIREEYPDRVMSTYSVIPSPKVSDTVVEPYNATLSVHQLVENADQCFALDNEALYDICFRTLKLTTPTYGDLNHLIAAAVCGTTCCLRFPGQLNCDLRKLAVNMVPFPRLHFFMVGYAPLTSRGSQQYRALTVPELTQQCFDAKNMMCAADPRHGRYLTCAVLFRGRMSSKEVDEQMLNVVNKSSSYFVEWIPNNVKASICDIPPKGLKMATTFVGNTTAVQETWKRVAEQFTVMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEEGEFDEDEMEG
|
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.
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Q9LKI8
|
C0QWM9
|
TYSY_BRAHW
|
Thymidylate synthase
|
Brachyspira
|
MQNYLDLLKKVLEEGEETKDRTGVGTRRIFGPQLRFKFEGNKIPIITTKRVFMKGVIIELLWFLQGSTNIKFLLENNVHIWDEWADDMGELGPVYGKQWRAWETKEGNKIDQISNIVNTLRNNPASRRIILNAWNVGEIDQMHLPPCHMMCQFSVNSKGGIITHLYQRSADLFLGVPFNISSYAILTRLLAMHSGLHASELIMTFGDAHIYNNHIEQVKLQLSREPLEQTTELFIDNRPNIFSHVYEDFKLEGYKYYPTIKAEVAV
|
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
|
C0QWM9
|
D2BJS8
|
TATC_DEHMV
|
Sec-independent protein translocase protein TatC
|
Dehalococcoides
|
MSSKNETPEVEEEEPPEEAKAKGKMPIGGHFNELRQRFTRGIIALVMGVMVAFFFATPIIGFLTAPGGPDFKPAQLGVMEYASVFFNVSLWAGFIIASPYILYQLIAFITPALNRNEKKFIFIAIPAVTVMFLAGLAFAYYVALPPALNILLHWGDDVVLTVVGIKDYMNVVTRILIALGLIFETPFIIMVLARLGVVSPQWLASKRKIWVVIAFVIAALITPTFDPVNQTIMAGPLIVLYEISIWLSKLVYRKKREVSESK
|
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.
|
D2BJS8
|
Q3KQE5
|
T38BA_XENLA
|
Transmembrane protein 38B-A
|
Xenopus
|
MESLSELSVQFSQLSMFPFFDMAHYVVSVMSAREQAGALDIAARSPMASWFSAMLYCFGGGILSSILLAEPPIAVLSNTTNIMLASTIWYMVYYFPYDLFYNCFFFLPIRLIIAGMKEVTRTWKILSGVTHAHSHYKDALLVMITIGWARGAGGGLISNFEQLVRGVWKPESNEFLKMSYPVKVTLIGAVLFTLQHGHYLPISRHNLMLIYTMFLVLIKVTMMLTHSTASPFLPLETPLQRILFGQRQKPSEVRQSASSSGAKGKPSKKTLDKDSGEQSKKKDS
|
Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores.
|
Q3KQE5
|
Q83II9
|
ULAA_SHIFL
|
Ascorbate-specific permease IIC component UlaA
|
Shigella
|
MEILYNIFTVFFNQVMTNAPLLLGIVTCLGYILLRKSVSVIIKGTIKTIIGFMLLQAGSGILTSTFKPVVAKMSEVYGINGAISDTYASMMATIDRMGDAYSWVGYAVLLALALNICYVLLRRITGIRTIMLTGHIMFQQAGLIAVTLFIFGYSMWTTIICTAILVSLYWGITSNMMYKPTQEVTDGCGFSIGHQQQFASLIAYKVAPFLGKKEESVEDLKLPGWLNIFHDNIVSTAIVMTIFFGAILLSFGIDTVQAMAGKVHWTVYILQTGFSFAVAIFIITQGVRMFVAELSEAFNGISQRLIPGAVLAIDCAAIYSFAPNAVVWGFMWGTIGQLIAVGILVACGSSILIIPGFIPMFFSNATIGVFANHFGGWRAALKICLVMGMIEIFGCVWVVKLTGMSAWMGMADWSILAPPMMQGFFSIGIAFMAVIIVIALAYMFFAGRALRAEEDAEKQLAEQSA
|
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II UlaABC PTS system is involved in ascorbate transport.
|
Q83II9
|
A0L833
|
TATC_MAGMM
|
Sec-independent protein translocase protein TatC
|
Magnetococcus
|
MNLDVEQKAPLVEHLIELRNRLMISVGAIIVGFILCYSFSEQIFEFLAAPLHEILGPQAKMIYTALHEAFFTQIKVSFFAGLFLAMPVLFTQMWLFIAPGLYQHERSAILPFLFVTPVLFFMGGTLAYYFVFPLAFKFFLGFQSSTIEALPSMREYLSLVIKLIIAFGITFELPVGLLLAIKAGVVSTAGLVDKRKYNIVLAFVAAAILTPPDPFTQVMLAIPIMLMYEISIFFGRGIERKRAEQEAAEEAQWAADHNVDDDDVDHPEHKA
|
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. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides.
|
A0L833
|
Q11HD9
|
TRMFO_CHESB
|
Folate-dependent tRNA(M-5-U54)-methyltransferase
|
unclassified Chelativorans
|
MTTKPIHVIGGGLAGSEAAWQAAEAGVPVILHEMRPVRGTDAHKTDGLAELVCSNSFRSDDAQTNAVGLLHAEMRLAGSLIMRAGDANQVPAGGALAVDRDGFSDAVTQAIHGHPLITVVREEVAGLPPSEWDQTIIATGPLTAPSLAEAIRQETGAEALAFFDAIAPIVHFDTIDMDTCWFQSRYDKAGPGGTGKDYINCPMNKEQYQAFVQALLDGEKTAFKEWEGTPYFDGCLPIEVMAERGPETLRHGPMKPMGLTNAHKPDEKAYAVVQLRQDNALGTLYNMVGFQTKLKYAEQVRIFRMIPGLENAEFARLGGLHRNTYINSPALLDITLQLKSRPGLRFAGQITGCEGYVESAAMGLMAGRFAAAARLGRKMMPPPATTAFGSLISHITGGHILSEDEPGKRSFQPMNVNFGLFPPVELPKPEGKRLRGKEKTLAKKRAITARALADCSDWLGVPTRAAAE
|
Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
|
Q11HD9
|
Q9XYU2
|
TCTP_PLAYO
|
Translationally-controlled tumor protein homolog
|
Plasmodium (Vinckeia)
|
MKVYKDIFTNDEVCSDSYIQEDPFGNPEFREIAFEVKSNKRIKGNDDYGIADNSEDAVDGMGADVEHVIDIVDSFQLTSTSLSKKEYSAYVKNFMQRILKHLEEKKPDRVDIFKTKAQPLIKHILTNFDDFEFYMGESLDMEAGLIYSYYKGEEITPRFVYISDGLFEEKY
|
Involved in calcium binding and microtubule stabilization.
|
Q9XYU2
|
P85109
|
VSP1_GLOBR
|
Snake venom serine protease
|
Gloydius
|
VIGGDECNINEHRFLVALYHSRSRTFLCGGTLINQEWVLTAAHCDRFFMYIRLGMHNKNVNFDDEQRRSPKEKYFFRCSNNFTKWDKDIMLIRLDSPVNNSAHIAPLSLPSNPPSVGSVCRVMGWGQTTSPQEDLSDVPRCANINLFNFTVCRAAYPWLPATSRVLCAGDMEGGIDTCNRDSGGPLICNGQFQGIVSKGQNLCAQPRKPALYTKVFDHLDWIQSIIAGNKTVTCPP
|
Thrombin-like snake venom serine protease. Cleaves bonds after Arg and Lys, converts fibrinogen (FGA and FGB) to fibrin and releases both fibrinopeptides A and B, and fibrinogen peptide Bbeta1-42. Has a blood clotting activity.
|
P85109
|
Q8XXY2
|
TRPA_RALSO
|
Tryptophan synthase alpha chain
|
Ralstonia
|
MSRIAQTFSQLSAQGRKGLIPFITAGDPYPELTVDLMHALVKGGANVIELGVPFSDPMADGPVIQRASERALAKKIGLRTVLDYVRAFRATDKTTPVVLMGYANPIERMGIDAFAKAASEAGVDGVLVVDYPPEECEAFAKTMRAAGIDPIFLLAPTSTEARMAQIARVASGYIYYVSLKGVTGAATLDLDSVAARIPQIRQHARLPVGVGFGIRDAATARAIGGVADAVVIGSRIVQLLEEASREQAVQCLTDFIADIRQALDA
|
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
|
Q8XXY2
|
A7NI03
|
TPIS_ROSCS
|
Triose-phosphate isomerase
|
Roseiflexus
|
MRTPLLAGNWKMYKTTGEARELVEGLLHGLGDVGDRKVLVCPPFTALQTVHDLVQGTPIALGAQDVYIEPQGAFTGAISPVMLRDLGCAYVIVGHSERRAIFGEGDELIGKKVRAALAHDLTPILCVGETKPQRDAGHAETVVVAQVRAALTGMTPEQIGRIVIAYEPVWAIGTGDTATPADAQAMHETIRRILGDMAGSDTAATINILYGGSVKPDNIDDLMAQPDIDGALVGGASLKADSFLRIVHFLSPQE
|
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
|
A7NI03
|
Q3YS67
|
TSAD_EHRCJ
|
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
|
Ehrlichia
|
MKKSVKVVLGIETSCDETAVAIVNSNKEVLSHKILSQKEHAEYGGVVPEIASRAHINYLYDLTVSCIEESQLSLNNIDAVAVTSGPGLIGGLIVGVMIAKGIASVTGKPIIEINHLEAHALIVRMFYEINFPFLLLIISGGHCQFLIVYNVGCYHKLGSSLDDSLGEVFDKVAKMLNLGYPGGPVIEKKSLSGDSKSFVLPRALTGRCGCDFSFSGLKTAVRNIIMNHEYIDNKLICDISASFQECVGDILVNRINNAIAMSKAIDKRIDKLVVTGGVAANKLLRERMLRCASDNNFEIFYPPSKLCTDNGIMIGWAGIENLVKDYVSNLDFAPKARWPLESLRSNIMKE
|
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.
|
Q3YS67
|
Q06493
|
YLH47_YEAST
|
LETM1 homolog
|
Saccharomyces
|
MLKYRSLPIKRAIHHPAPGITPISPRIMVSRLRVIPSFNLKFNRWNSSVPESSKKELKTTDGNQESASKVSPVKEKEKVPFKVKMQKALRHYWDGSKLLGLEIKISSKLLMKSAAGYPLTRRENLQLKRTTQDIVRLVPFAAFLIIPFAELLLPFALKLFPNLLPSTYESSKKRENKLENLRNTRKLMSEIIKNNKSHFKPNNISEEQKALFNRFYTHVRATGVPESRQQLIEVARLFTDDTVLDNVTRPYLIALAKYMNLQPFGTDVMLRYRIRYKMLELKKDDLSIYYEDAEQLSLSELKTACASRGIRSVDVEPSVLYSNLRLWLNMRLKDKIPSTLLIMATAYNYGNVQSKESLYDALCDVLIGIPDELYHEVKVNVVKEDEASAKQKLKQLREQEEIMKEEEQQEENAIVSVKDELSLDDQDKNIDAAAPDVKPHDTKPIGEAAAIKEK
|
Involved in mitochondrial potassium homeostasis through the mitochondrial K(+)/H(+) exchange regulation.
|
Q06493
|
Q39QN3
|
UVRC_GEOMG
|
Excinuclease ABC subunit C
|
Geobacter
|
MFDKSRLNTLPESPGVYLMKGSDGTILYVGKAKSLRKRVRSYFGAAGESRYHIRFLVARVAEVEVIVTDTEKEALILENTLIKKHRPRYNLDLRDDKTYFSLRMDMNEEFPRLTIIRKVRQDGARYFGPYSSAASAREALKQLYRLFPLRHYPLETCRRRRRPCLFYQLRQCSAPCHGLISPEEYQGLVQGAALFLDGKNRDLLKTYRERMASAAANERYEEAARYRDLIRAIEVTVEKQKMVTTGGDADVLGIHREGSSLSLALLFIRGGRLIGSRSYLLAWELEDEEAVSSFLNDYYSREVFIPDEVLVPLPVADSAALAELLSERRGKRTSVAHPQRGTKAGLVKLAGKNAEAALREKQKREEGAEAVLTELKERLHLRNLPRCIECYDISNIQGTYPVGSRVSFRDGKADKGGYRHYRIKTVAGADDFAMMHEVLSRRFRDSPAKDEHPDLIVVDGGIGQLNILTAVLRELQVEDVDAASLAKSRVERDMAAEELTRSTERVFLPGRKNPVILRQNSAPLLLLARIRDEAHRFAITYHQKLRGKDTIRSILDTIPGIGPKRRKELLRQFGSLRRIREASRDELAATPTIPPTLAESIWKSLHENDEGDTP
|
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.
|
Q39QN3
|
B3DRW0
|
TPIS_BIFLD
|
Triose-phosphate isomerase
|
Bifidobacterium
|
MASKRIPLVAGNWKMNFDHLEATYFVQKLVWLLRDAHFDFKRCEVALFPSFTSLRSVQVLVEADKLHVAYGAQSVSVTTQGAFTGDVSADMIAHLGCSYVIVGHSERRKYHPEDDANIVDQVRAVLAAGMQPILCVGESFEERRQGIELDFAVGQVRDVTRDLNEEQAAKLIVAYEPVWAIGTGMVATPQSAQDAANAIRNDLKTTFGTKVSDSVRILYGGSVTSKNAAELISQPDVDGFLIGGAALDVEELAKIARLALKSTKSRN
|
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
|
B3DRW0
|
O43033
|
YGU4_SCHPO
|
Uncharacterized methyltransferase C3B9.04, mitochondrial
|
Schizosaccharomyces
|
MGILKKTIFIGGIYGLGVYIGAVAWRLRKDVLNYESRQKSDLLIPNSNSISIYNQIADKYSRKITREEIFSGIYFLRYFLLRNAKGDVLEVGSGPGTNFPFYKWKKINTLTLVEPAEKMREIADARAKKKVPPNVLYRQFADLRQLPPNQSYDTIIQTFCICSQEKAVEQLNNYRSLLRSDGRILLIEHGKGKYKFLNRILNAYAESHYESWGCVWNRDIEQLLEDSELTIDSCKRFNFGTTYVIEAH
|
Probable methyltransferase.
|
O43033
|
Q73S79
|
Y4197_MYCPA
|
Putative S-adenosyl-L-methionine-dependent methyltransferase MAP_4197c
|
Mycobacterium avium complex (MAC)
|
MTRTDQDSWDLASSVGATATMVAAARALASTGERPIINDPFAAPLVRAVGLDFFRRLVDGEVAPADPQRGERDLQLETDSIAVRTRFFDDFFTGAARDGIRQSVILAAGLDARAYRLDWPAGAVVYEVDQPKVVEFKTNTMAALDARPAAQLRTVSIDLREDWPEALRANGFDVTQPTSWSAEGLLMYLPPEAQDRLFDNITALSAPGSRLATEYHPDATGTTMAQRAQEFNDRWARVGCDIDLSGLFFDGERSNVVEYLTGRGWRVSARPRRDLFDDYGLAYPEDDETAQFPNIVAVSAELG
|
Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity.
|
Q73S79
|
Q7N9T4
|
YIHI_PHOLL
|
Der GTPase-activating protein YihI
|
Photorhabdus
|
MNPLKKKAPAKVSASKQKRKNREELNAEGRARKREKKHRGNPPGNRNQEQSGDKHPSGKQQRDPRLGSKVPVPLIVGEQPTKPVVANKVETKPRLSPQEELAMLENDDRLDALLERLENGESLSKEEHAYVDTTLDRIDALMEELGIKLDEEEREEEKQDDIMQLLKGN
|
A GTPase-activating protein (GAP) that modifies Der/EngA GTPase function. May play a role in ribosome biogenesis.
|
Q7N9T4
|
Q9PJS0
|
YIDD_CHLMU
|
Putative membrane protein insertion efficiency factor
|
Chlamydia
|
MKTSWIKIFFQGMIHLYRWTISPLLGSPCRFFPSCSEYALVALKKHPLKRSLFLIANRLLKCGPWHIGGIDLVPGTSIEEYLESPDDKNVPPDQETV
|
Could be involved in insertion of integral membrane proteins into the membrane.
|
Q9PJS0
|
Q2NL26
|
TKTL1_BOVIN
|
Transketolase 2
|
Bos
|
MADAEASATMADEAKPDSKTLQILRDMANRLRIHSIRATCASSSGHPISCSSAAEIMSVLFFHVMRYKQADPKNPDNDRFILSKRLSFVDVATGWLGQGLGAACGMAYTGKYFDKASYRVFCLVGDVESWEGSVWEALAFASHYSLDNLVAIFDVNRLTHSTTLPLEHSIDVYQKRCEAFGWNTLVVDGRDVEALCQVFWQAAQMKNKPTAVVAKTFKGRGIPSVEDAENWHGKPMPKERADAIIKLIESQIETNKSLEPKAPIEDSPQINISVIEMTSPPDYEISDVIATRKACGLALAKLGHANDRVIVLDGDTKNSTFSDIFKREHPERFIECFIAEQNMVSVALGCVTRGRTVAFACTFAAFLTRAFDQIRMGGISQTNINLIGSHCGVSIGEDGPSQMALEDLAMFRAIPNCTIFYPSDAISTEHAVFLAANIKGMCYIRTSRPETAIIYTPQESFEIGQAKVIRQSVNDKITVVGAGITLHEALAAADDLSKQGISLRVIDLFTVKPLDAATIISNAKATGGQIITVEDHYPEGGIGEAVSAAVSMEPDIVVHHLAVSGIPRSGKPSDLLDMFGISSKHIIWAVERILMK
|
Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
|
Q2NL26
|
B1VSW9
|
UREG2_STRGG
|
Urease accessory protein UreG 2
|
Streptomyces
|
MRHGHPPTDIHHGINQGEPMDDNVLRVGIGGPVGSGKTALIEALVPVLIERGHRPAVITNDIYTQEDAQHVRRTLAGVLEPERVVGVETGACPHTAVRDDPTMNLAAGAEMLERFPDTDTLLYESGGDNLTLTFSPALVDLFLFVLDTAEGEKMPRKRGPGITESDLLVINKIDIAQYVRTDIGIMEADAHRVRDDRPVVLTDCLTGVGIDDIALYLESRRKVLI
|
Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG.
|
B1VSW9
|
Q495A1
|
TIGIT_HUMAN
|
V-set and transmembrane domain-containing protein 3
|
Homo
|
MRWCLLLIWAQGLRQAPLASGMMTGTIETTGNISAEKGGSIILQCHLSSTTAQVTQVNWEQQDQLLAICNADLGWHISPSFKDRVAPGPGLGLTLQSLTVNDTGEYFCIYHTYPDGTYTGRIFLEVLESSVAEHGARFQIPLLGAMAATLVVICTAVIVVVALTRKKKALRIHSVEGDLRRKSAGQEEWSPSAPSPPGSCVQAEAAPAGLCGEQRGEDCAELHDYFNVLSYRSLGNCSFFTETG
|
Binds with high affinity to the poliovirus receptor (PVR) which causes increased secretion of IL10 and decreased secretion of IL12B and suppresses T-cell activation by promoting the generation of mature immunoregulatory dendritic cells.
|
Q495A1
|
B5ZAX5
|
Y158_UREU1
|
UPF0122 protein UUR10_0158
|
Ureaplasma
|
MLNKNKRWYLIALYDIYQGLLTTKQCEYFNLHYFKDLSFSEIAELKEVSKSAISDCLNKVCDQLLKYEQALLIYEKNKKRNDLYTLINDSELVKKLKDI
|
Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein.
|
B5ZAX5
|
Q6FQJ1
|
VPS27_CANGA
|
Vacuolar protein sorting-associated protein 27
|
Nakaseomyces/Candida clade
|
MATTSSEEFSEVIERATSESIPNGELNLPVALEISDILRSRRIAPKDGMRCLKKRITNTTNNPNTQLSSWKLVEICIKNGGIPFLREICSREFMDTMEHTILKYDDSDEVVELVTTMLYELYLAFQNDSQLNYVSRVYDKLRQRGVKFPEGAPISSNVNALFDSKTPADWIDSDACMICSKKFSLLNRRHHCRSCGGVFCQDHSSKSIPLPDLGIYDSVRVCDNCYDDYDYKKGSGSQGKKRKHRKSHRHATEDEDEDLRKAIELSLRASNSSVEPVIPVVESEPQIPAVEEEDPDLKAAIEASLREAEEEKRRREEHAQQQNTNAYPQQFRPPANELTPADEEDIYLFASLVERMKTRPPSEILDDPQLQQLAQKVFASKPRLGNTLNSKIQKYNTLVDMNGKISHIMNTYDNLLEQELRNINLSERFNVPQAQADPYSQYSQYNQPAIQNNTSQTNNVVNNKPLSQRESEPQYTAPTDSQTIESKAYERQLENLVQPPSNVNNERVASEPPYPNEELNDITSIQLNSERAGKYEENAVPPGSIPYPIENDDQDETTRTKKNDNITNFDFPTVPARKLPENNVEQVEDKPQDSQEEALLIEL
|
Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB) and recruits ESCRT-I to the MVB outer membrane.
|
Q6FQJ1
|
Q55GQ6
|
UPP_DICDI
|
UMP pyrophosphorylase
|
Dictyostelium
|
MSYPENVVVLKSNHQLKGLFTIIRNRETKREDFIFYSDRIIRLLIEEGLYCLPFHETTITTPTGCEYQGVTFASKICGVSIVRAGESMEAGLRAVCKHIKIGKILIQRDEETALPKLLYAKLPHDIANRQVLLLDPMLATGGTVTQAVEVLLERGVKEENIVFINLVASPEGIKVFTDKYPRVKVVTGEIDSHLNEKKYIIPGLGDFGNLYFGTED
|
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
|
Q55GQ6
|
P84035
|
VM3BA_BOTAS
|
Snake venom metalloproteinase basparin-A
|
Bothrops
|
SHDNAQLLTAIKAYIATMCDPKMAVIMAHEIGHGGYYGYCRKIPCAPEDVKDDDIGMVLPGTK
|
Snake venom zinc metalloproteinase that catalyzes the conversion of prothrombin (F2) to alpha-thrombin through formation of a thrombin intermediate, without requiring additional cofactors. Also inhibits collagen-dependent platelet aggregation in vitro, an effect that does not depend on proteolytic activity. In vivo, at low doses, induces defibrin(ogen)ation when injected intravenously or intramuscularly into mice. At higher doses, causes sudden death by intravenous administration due to numerous occluding thrombi in pulmonary vessels.
|
P84035
|
A3QD46
|
TOLB_SHELP
|
Tol-Pal system protein TolB
|
Shewanella
|
MKNLGRWLILGLAFLTIPAKAALDIVITEGVDAARPIAVVPFVWQGSTPMPQQISDVVMSDLTRSGTFKPMDELGLPQRNLGSLAQMDLKAWSNVAAEAVVMGTVKPYGPDQYLVNFELIDLVKAQMQSGGPQSASEYLLDSRETVISSAQFRQYGHRISDIVYEKLTGIRGAFLTRIAYVVVDHKAKSPYKLMIADYDGYNEQMLLRSPEPLMSPAWSPDGRRLAYVSFENKQAEVFVQDIYTQQRTKVTSFPGINGAPTFSPDGKKLALTLSKDGQPEIYVADIATKAIKRVTNHYAIDTEASWTPDGKSLIFTSERGGRPQIYQVALASGKVTRLTFEGEWNLGGSISPDGRSMVFVNRTNGKFNIARMDLETRFMQVLTTTRLDESPSIAPNGTMVIYGTTYQGQQVLAAVSMDGRFKARLPVGQGEVKSPAWSPFL
|
Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
|
A3QD46
|
B4RY55
|
UBID_ALTMD
|
Polyprenyl p-hydroxybenzoate decarboxylase
|
Alteromonas
|
MKYKDLRDFIRQLEAKGELVRISQPIDTDLEMTEIADRTLRAGGPALLFENPKNHDMPVLANLFGTPERVAMGMGQESVEALREVGKLLAYLKEPEPPKGLKDLWEKLPVFKQVLNMPAKVLKKAPCQEVVLTGDDVDLSKIPVQRCWPGDAAPLVTWGLSVTKGPHKKRQNLGIYRQQVIGKNKLIMRWLSHRGGALDFREWCQTHPGEPYPVSVALGADPATILGAVTPVPDTLSEYAFAGLLRGDKTEVVKSISNDLQVPASAEIVLEGYIAQDETAPEGPYGDHTGYYNEVDDFPVFTVTHITHRKDPIYHSTYTGRPPDEPAILGVALNEVFVPILQKQFPEIVDFYLPPEGCSYRMAVVTMKKQYPGHAKRVMMGVWSFLRQFMYTKFVIVCDDDVNARDWNDVIWAITTRMDPARDTVMIENTPIDYLDFASPVSGLGSKMGMDATNKMPGETDREWGVPIVMDEGVKKRVDDIWDSLGIM
|
Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis.
|
B4RY55
|
Q7CRQ0
|
URODH_AGRFC
|
Hexuronate dehydrogenase
|
Agrobacterium tumefaciens complex
|
MKRLLVTGAAGQLGRVMRERLAPMAEILRLADLSPLDPAGPNEECVQCDLADANAVNAMVAGCDGIVHLGGISVEKPFEQILQGNIIGLYNLYEAARAHGQPRIVFASSNHTIGYYPQTERLGPDVPARPDGLYGVSKCFGENLARMYFDKFGQETALVRIGSCTPEPNNYRMLSTWFSHDDFVSLIEAVFRAPVLGCPVVWGASANDAGWWDNSHLGFLGWKPKDNAEAFRRHITETTPPPDPNDALVRFQGGTFVDNPIFKQS
|
Catalyzes the oxidation of D-galacturonate and D-glucuronate to galactarate and D-glucarate, respectively. In fact, in water solution the substrate D-galacturonate is predominantly in pyranosic form whose beta anomer is converted by the enzyme to D-galactaro-1,5-lactone; in solution, this reaction product rearranges to the more stable D-galactaro-1,4-lactone. Makes part of the oxidative degradation pathway of D-galacturonate, which allows A.tumefaciens to utilize D-galacturonate as a sole carbon source. Cannot use NADP(+) instead of NAD(+) as cosubstrate. Is not active on D-galactose, D-glucose, D-galactonate and D-gluconate.
|
Q7CRQ0
|
Q6PVW7
|
ZPBP2_CHICK
|
Zona pellucida-binding protein 2
|
Gallus
|
MAGGGGRPCSPQRALLGMVAIMAVVAEARWGAPGRARAAPEEDQISVGFFRKNVIYGNVRRAENVYVKMFTNSPSLVCMDLSLSQEEIIDPKYSWTGPDGRNLEGRGYANLTGSGELMLVGFQESMSGAYTCTLSHRIIETSAQEEVDVRDTYRFMVYAYREANHVYQVSVRFTAKGCELAANARFVEELKKIMESLISDLTCGVKGPSYRCHSLEAPHRGSPSELFITFQVNPFAPGWEDLCSRLPQDCEDTTNRRAQEATERIGEFFRKQTYALKHQFQTVPTIHYVEGSFSVTPIDSCRPGFGRNNITHRSCAGCCVVCSPGTYSPDSAGSCRVCAGRRTAGYGAKSCP
|
May be implicated in the gamete interaction during fertilization.
|
Q6PVW7
|
P04185
|
UROK_PIG
|
Urokinase-type plasminogen activator chain B
|
Sus
|
MRVLRACLSLCVLVVSDSKGSHELHQESGASNCGCLNGGKCVSYKYFSNIQRCSCPKKFQGEHCEIDTSQTCFEGNGHSYRGKANTNTGGRPCLPWNSATVLLNTYHAHRPDALQLGLGKHNYCRNPDNQRRPWCYVQVGLKQLVQECMVPNCSGGESHRPAYDGKNPFSTPEKVEFQCGQKALRPRFKIVGGKSTTIENQPWFAAIYRRHRGGSVTYVCGGSLISPCWVVSATHCFINYQQKEDYIVYLGRQTLHSSTHGEMKFEVEKLILHEDYSADSLAHHNDIALLKIRTDKGQCAQPSRSIQTICLPPVNGDAHFGASCEIVGFGKEDPSDYLYPEQLKMTVVKLVSHRECQQPHYYGSEVTTKMLCAADPQWKTDSCQGDSGGPLVCSTQGRLTLTGIVSWGRECAMKDKPGVYTRVSRFLTWIHTHVGGENGLAH
|
Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin.
|
P04185
|
Q6G5P5
|
TILS_BARHE
|
tRNA(Ile)-lysidine synthetase
|
Bartonella
|
MCVRLAGNLFKTSDFIQCQKLILAVSGGSDSLALLFLVKDHLKTLSVPPEIIVVTVDHQLRQESAREASIVAEICRAHHIQHRIVRWEGKKPKTHIASSARVARYDLLFQEAQKQGATLIMTGHTLNDQVETYQMRYQRLQKSADVLQQEAFAEMGGGVHADVLQQEAFAERCERMGVGGHGGDIAEKSDGLIYERGLSCIPREALLRGTVRLIRPLLGVKRETLRTYLRLKEKTWIEDPTNEDCNFERVRVRQSLQPKKFTCIARKVHEAALQRRQQAKNIADLILALDITVEYGRCFIAKPALFLQKHPGFPFVVGLFAVLMGGGFYLLPHKKLSTLVQKLSLHSSEKRRFTYAGSVIEYNRSGIAFWREARNIKEAIVEKGQTFLWDGRYQITNHSHEPIKVGAAGLQQLKSLFKNNNFNLENTHFPSLKSLLMISNDKGYDIPELAYHAAMQHTITIRRIMAPFDWLLSSQDAAFVNVVQPFFDIKVKG
|
Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
|
Q6G5P5
|
Q8T3S6
|
TXAA2_ARAVE
|
Toxin 2
|
Araneus
|
MALALLGLTIKPEHVPEGTGKAVADVEALACDPAQCMRSCPFNPFLNQYGGICKNGQCVCVKPS
|
Putative insecticidal toxin.
|
Q8T3S6
|
Q820E4
|
TRMD_CHLCV
|
tRNA [GM37] methyltransferase
|
Chlamydia
|
MEIEILSLFPDYFDSPLRSSILGKAIKNGLLKIQSRDIRDFGLGKWKQVDDAPFNNDGMLLMAEPVVQAIRHIKRSDSRVIHLSPQGKPLTAQKSRELAKCSHLIFLCGHYEGIDERALESEVDEEISIGDYVLTNGGIAALVVIDALSRFIPGVLGNQESAEKDSLENGLLEGPQYTRPRVFEGKEVPEVLLQGDHQAVARWRKQVSLDRTRERRPDLYIRYLYDRENEEVFPREEDTKQSTLEGESAVVLEVEDLQRSRKFYSKMFRLNQPSKDKLQIPGRTQMVLHLQEVGLKNKNTAILSLRLDCEDDFFSFLGRWKMLGGTLEQADDHGTVRLVRDFDGHQWTISYKKVK
|
Specifically methylates guanosine-37 in various tRNAs.
|
Q820E4
|
Q0DKN3
|
VLN1_ORYSJ
|
Villin-1
|
Oryza sativa
|
MKGVDDAFLGVGDKPGLDIWCIMGSNLIAIEKSLHGKFYTGNTYIILSTVELKSGVRQHNVHYWVGEEAKEEDCLTASDKAIELDVALGSNTVQYRETQGEESDKFLSYFKPCIIPIQGSLSSHMRIYGDKSKDTTMFRCEGEHVARVTEVPFSRSSLDHKAVFVVDTESKIFLFSGCNSSMQTRAKALDVVKHLKENRHCGRCEIATIEDGKLVGDSDAGDFWNLFGGYAPIPRDVQDTVMTELMTTSSKKLFWINKRNLVPVETNLLEREMLNSDRNYILDCGTEVFLWMGMTTLVSERRTSVTALEDYVRCEGRQSNARSVILTEGHETVEFKMHFQHWPKNAVPKLYEAGREKVAAIFKHQGYDVTEIPEDKPRHFISCNGSLKVWLVDNGSVTLLCTEEQEQLYNGDCYIIRYSYIEDGKDYHLFFAWSGLNSINEDRVAAASLMSGMIDSVKGHAVVAQVFEGREPEMFFLVFKSLIIFKGGRSMAYKNFVSQRSDANGWYQKNGVALFRVQGLKHDCIRAIQVDLAASSLNSSHCYILQAGGSFFTWLGSLSSPSDHNLLDRMMDKLCPLKQSLLVREGSEPDRFWEALGGRSEYLREKQVKDWPADPHLYTCHFEQGLFKAKEVFSFSQDDLVTEEILILDCVEELHIWVGHQSGVLSKEQALDIGKMFLQAGIHQDGRRPIDTTMYIVTEGDEPRFFTSFFNWDYSKQTMLGNSFERKLAILKGISQKLETPERSLRKSSSSSLPRRSPGTSSSEPTTPEQRAAARTFASASTGKLLRERSPAALSPSLSTPSPSPRSRSSASSSPASWNSTPSTVARRLFPPSLHASAEAVATGTPRRR
|
Ca(2+)-independent actin-binding protein. Binds actin microfilaments (MFs). Involved in actin filament bundling, severing and capping. Caps the barbed end of actin filaments and protects them from disassembly. Promotes VLN3-mediated MF severing.
|
Q0DKN3
|
P24055
|
TF_RABIT
|
Coagulation factor III
|
Oryctolagus
|
MAPPTRLQVPRPGTAVPYTVLLGWLLAQVARAADTTGRAYNLTWKSTNFKTILEWEPKSIDHVYTVQISTRLENWKSKCFLTAETECDLTDEVVKDVGQTYMARVLSYPARNGNTTGFPEEPPFRNSPEFTPYLDTNLGQPTIQSFEQVGTKLNVTVQDARTLVRRNGTFLSLRAVFGKDLNYTLYYWRASSTGKKTATTNTNEFLIDVDKGENYCFSVQAVIPSRKRKQRSPESLTECTSREQGRAREMFFIIGAVVVVALLIIVLSVTVYKCRKARAGPSGKESSPLNIA
|
Initiates blood coagulation by forming a complex with circulating factor VII or VIIa. The [TF:VIIa] complex activates factors IX or X by specific limited proteolysis. TF plays a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade.
|
P24055
|
Q7VFX7
|
UVRB_HELHP
|
Excinuclease ABC subunit B
|
Helicobacter
|
MGKFILDSQFAPAGDQPQAIQKITQFIHNGAQYSTLVGVTGSGKTYTMANIIANLNIPTLIMTHNKTLAAQLYSEFRGFFPKNHVEYFISHFDYYQPEAYIPRRDLFIEKDSSINEDLERLRLSATTSLLAYDDIIVIASVSANYGLGNPAEYLTMIHKFEIGQEEAQKTLLLKLVDMGYTRNDTIFERGNFRVNGEVIDIFPAYNEKEFIRIEFFGDEIERIGVFDALERTALTQLESFVLYAANQFIVGAQRLQSAIKNIEVELENRLEEFVSQDKQIEYQRLKTRTEFDLEMIKESGICKGIENYARHLTGKKAGETPYSLLDYFEQKGKPYLLIVDESHVSLPQFGGMYAGDRSRKEVLVEYGFRLPSALDNRPLRFDEFINKAPHFLFVSATPAQKELELSQEHIAEQIIRPTGLLDPLYEVRDADNAVLDLYDEIKARIAKNQRVLITTLTKKMAEELSKYYAELGIKVRYMHSDIDAIERNHLIRALRLGEFDVLIGINLLREGLDLPEVSLIAIMDADKEGFLRSETSLIQTMGRAARNVEGKVILYAKKITGSMQRAFEVTDYRRTKQEEFNRIHNITPKSVQRNVEQELKIESSGLSRLYEKASKKIPKSERESIIKELNIKMHQAAKALEFEEAARLRDEIARIRTM
|
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by UvrC and the second UvrB is released. If no lesion is found, the DNA wraps around the other UvrB subunit that will check the other stand for damage.
|
Q7VFX7
|
A5D3C3
|
YQGF_PELTS
|
Putative pre-16S rRNA nuclease
|
Pelotomaculum
|
MRIMGLDLGDKKIGVALSDPMGWTAQGLDVIAVKGPPEASVERISELVRQYGVGKIVVGLPRNMNGSFGPRAERARAFAGCLAGALNLPVELWDERMTTLEAEKLLIEADLSRARRRQVIDKMAAVLILQSFLDSQGRPRREAGGKNPGGPEEP
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
|
A5D3C3
|
Subsets and Splits
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