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
|
|---|---|---|---|---|---|---|
Q6DTN4
|
HYUC_RHIML
|
L-N-carbamoylase
|
Sinorhizobium
|
MAAPGENRRVNADRLWDSLMEMAKIGPGVAGGNNRQTLTDADGEGRRLFQSWCEEAGLSMGVDKMGTMFLTRPGTDPDALPVHIGSHLDTQPTGGKFDGVLGVLSGLEAVRTMNDLGIKTKHPIVVTNWTNEEGARFAPAMLASGVFAGVHTLEYAYARKDPEGKSFGDELKRIGWLGDEEVGARKMHAYFEYHIEQGPILEAENKQIGVVTHCQGLWWLEFTLTGREAHTGSTPMDMRVNAGLAMARILEMVQTVAMENQPGAVGGVGQMFFSPNSRNVLPGKVVFTVDIRSPDQAKLDGMRARIEAEAPKICERLGVGCSIEAVGHFDPVTFDPKLVETVRGAAEKLGYSHMNLVSGAGHDACWAAKVAPTTMIMCPCVGGLSHNEAEDISREWAAAGADVLFHAVLETAEIVE
|
May be involved in the asymmetric conversion of racemic 5-substituted hydantoins to the corresponding L-amino acids. Catalyzes specifically the conversion of N-carbamoyl-L-amino acids to free L-amino acids in an irreversible reaction. N-carbamoyl-L-methionine is the best substrate. HyuC of R.meliloti is the first L-N-carbamoylase that hydrolyzes N-carbamoyl-L-tryptophan as well as N-carbamoyl-L-amino acids with aliphatic substituents.
|
Q6DTN4
|
Q9HGI4
|
ERF3_ZYGRO
|
Translation release factor 3
|
Zygosaccharomyces
|
MSDPNQNGQQGGQQNAGGNYYQQYFQKLTQQAQAGGGYQPYGGYGGYGGYGGYQPYGGYQQFYQDGQQAQQGAYNGYPYQAQGAPGGFNNYNNQFQPQQQSQGMTLDDFHKQKQTSQSAPPKQKKSLKLVSSSGIKLANATKKPKEDEKKEEEPKKEEKKAEPKEQESKKEEPKREGTPRPAAAKDEKKEDLPKLEKLKIKEEQAAANASGADSLIKEQEEEVDEGVVNDMFGGKDHMSIIFMGHVDAGKSTMGGNILYMTGSVDKRTVEKYEREAKDAGKQGWYLSWVMDTNREERDDGKTIEVGRAYFETEKRRYTILDAPGHKMYVSEMIGGASQADVGILVISARKGEYETGFEKGGQTREHALLAKTQGVNKLIVTINKMDDPTVNWSKERYDQCVKNLSNFLKAIGYNVKEEVVFMPVSGYSGAGLGTRVDPKECPWYDGPALLEYMDNMSHVDRKMNAPFMLPIAAKMRDMGTIVEGKIESGHIRKGHSTLLMPNKIPVEIQNIYNETENEVDMAICGEQVKLKIKGVEEEDIAPGFVLTSPKNPVKNVTRFVAQVAIVELKSILSSGFSCVMHVHTAIEEVRITKLLHKLERGTNRKSKKPPAFAKKGMKIIAVLETERPVCVETYQDYPQLGRFTLRDQGTTIAIGKIVKIIE
|
Involved in translation termination. Stimulates the activity of ERF1. Binds guanine nucleotides.
|
Q9HGI4
|
P17934
|
PA2A4_BUNMU
|
Phosphatidylcholine 2-acylhydrolase
|
Bungarus
|
MNPAHLLVLSAVCVSLLGAANIPPQHLDLYQFKEMIRYTIPCEKTWGEYADYGCYCGAGGSGTPIDALDRCCYVHDNCYGDAANIRDCDPKTQSYSYKLTKRTIICYGAAGTCARVVCDCDRTAALCFGNSEYIEGHKNIDTARFCQ
|
Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
|
P17934
|
Q1CCJ6
|
RNPA_YERPN
|
Protein C5
|
Yersinia
|
MVKLAFPRELRLLTPSHFTFVFQQPQRAGTPQITILGRLNELGHPRIGLTVAKKHVKRAHERNRIKRLTRESFRLHQHALPSMDFVVLVKKGVADLDNRALTEALEKLWRRHCRQAPAS
|
RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
|
Q1CCJ6
|
Q5PBH2
|
EFG_ANAMM
|
Elongation factor G
|
Anaplasma
|
MSSKGDLSRCRNIGIMAHIDAGKTTTTERILFYTGKQNRIGEVHEGAASMDWMEQERERGITITSAATTCFWNDCRINIIDTPGHVDFTIEVERSLRVLDGAVAVFDGVAGVEPQSETVWRQADKYDVPRICFVNKMDRIGADFYACVDMIKDRLGAVPLVLQLPIGVDKSFVGVVDLVEMRSITWEEDSLGAKFNYGEIPSDLMEKAQDYRARLIESAVEMNDEAMNLYLDGGEISVPLLKSCIRSGVIGAKFVPVLCGSAFKNKGVQPLLDAVVDFLPSPSDIPTIEGASASDPQKAVTIKSSVDDKFVALAFKVMVDRFVGSLTFIRVYSGKLTGKSVVLNSAKGVTESVGRILRMHANNREDISEIQAGDIAALAGLKKTTTGDTLCDQNFPVVLEKMDFPESVMEIAVEPVSTADQEKMGTALSRLVAEDPSLKVCVNSESGQTILKGMGELHLEIIVDRMKREFGVEASVGAPQVAYRETITKSAEIEYVHKKQTGGAGQFAKVNILFEPLPPGSGFEFENKITCGAIPKEYIPGVQSGLELVKETGMIAGFPVIDFKATLFDGAFHEVDSSPLAFELAAKGAFREMANKAGPVLLEPIMRVEIITPDEYMGDVIGDVNSRRGRVAEMQDRHNAKLITAFIPLGKMFGYVKDLRSMSQGRAQYSMYFARYERVPENAVDNVMKK
|
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
|
Q5PBH2
|
Q821T4
|
IPYR_CHLCV
|
Pyrophosphate phospho-hydrolase
|
Chlamydia
|
MSEKPSLSIMHPWHGPILTQDNYESLCCYIEITPQDSVKFELDKATGLLKVDRPQKFSNFCPCLYGLLPRTYCGELSGKYSGEQSLKENIQGDDDPLDICVLTEKNITHGNILLQARPIGGLRIIDSGEADDKIIAVLEDDLVFSEIQDISDCPCTVLDMIQHYFLTYKASPEHLIHGKPAKIEIVGIYGKKEAQKVIELAHQDYLNKFCREKTTI
|
Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
|
Q821T4
|
B1XKF6
|
DAPAT_SYNP2
|
LL-diaminopimelate aminotransferase
|
unclassified Synechococcus
|
MVRINENYLKLKAGYLFPEIARRVNGFLAENPNAPIIKLGIGDVTEPLPAACREAMAKAIDDMGDRANFKGYGPEQGYAWLREKIAAHDFQARGCDIDASEIFVSDGAKCDTGNILDIFGKDNTIAVTDPVYPVYVDTNVMAGHTGEADESGKYGGLTYIPITADNDFVAQIPTEKVDLIYLCFPNNPTGATATKEQLQAWVDYAKTNGSIIFFDAAYEAFITDESLPHSIYELEGAKDCAIEFRSFSKNAGFTGTRCAFTVVPKNLTVTASNGQAVQLWSLWNRRQSTKFNGVSYIVQRGAEAVYSEAGQAQIKTLIDFYLENAAIIRRELQAVGFDVYGGVNAPYVWVKTPAGLSSWDFFDKLLINCNVVGTPGSGFGAAGEGYFRISAFNSRENVLEAMKRITTAFQ
|
Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate.
|
B1XKF6
|
A6V389
|
LEXA_PSEA7
|
LexA repressor
|
Pseudomonas
|
MQKLTPRQSEILSFIKRCLEDHGFPPTRAEIAQELGFKSPNAAEEHLKALARKGAIEMTPGASRGIRIPGFEPHAANDDEGLPVIGRVAAGAPILAEQNIEESCRINPAFFNPRADYLLRVRGMSMKDIGILDGDLLAVHVTREARNGQVVVARLGEEVTVKRFKREGSKVWLLAENPEFAPIEVDLKEQELIIEGLSVGVIRR
|
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
|
A6V389
|
Q9USM7
|
TIM23_SCHPO
|
Mitochondrial import inner membrane translocase subunit tim23
|
Schizosaccharomyces
|
MSWLFTRNKEEEPTSKIDSSELQVPTEATASDILSGSEFDPAKLHPLADLDKPLDYLLIEEDALSTLPGDSMAIPSRGWQDDLCYGTGTSYLSGLAIGGLWGLNEGMKKTKDITSTRLRLNGILNGVTRRGPFVGNSLGVLALVYNGINSLIGYKRQKHGWENSVAAGALTGALYKSTRGLRAMAISSSLVATAAGIWTLAKRSFTKRLN
|
Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
|
Q9USM7
|
Q5X0P0
|
ATPD_LEGPA
|
F-type ATPase subunit delta
|
Legionella
|
MSDSTTIARPYAKAIFEHALAEKKLSEWSEYLTLLAQVVLTPQATQFIANPASTDEQQIELLIEICGSKFKKNDALNNLIKLLTTNKRLMLLPEIKALYEVYRAEQEKILEVDVVSYSELTPAQQQRLSESLSQRLSRKVSLKISIDPSLLGGALIRAGDLVIDGSVRGKLNMLGTSLAA
|
This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
|
Q5X0P0
|
Q71Y88
|
AROB_LISMF
|
3-dehydroquinate synthase
|
Listeria
|
MPEITVRAKSKTYPVYINEFALEDVREKWTESLAKFSHVFVLTDEHVAELHQAKLDAVLADLPVVTYYVAPNGEEAKTFRVYEDVMTKLIETGLDRKAVLIAFGGGVIGDLGGFVAATYMRGIPFYQVPTTVLAHDSAVGGKVAINHPLGKNMIGNFYQPEAVIYDTQFFATLPEREMRSGFAEMIKHALISDQTLLRALMDTFTEPKDFYTKDLTPFLQRGIEIKANIVAQDETEQGVRAYLNFGHTFGHALEAYGNFGKWLHGEAITYGMIYALTMSETIYGLDFDLAEFKTWLKQLGYDTTFDATVPFNKILENMRHDKKTTFNEISMVLLEEIGEPVIFKAEDDLIFETYKRVMRNGGNGI
|
Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
|
Q71Y88
|
Q3J3V1
|
SELO_CERS4
|
Protein adenylyltransferase SelO
|
Cereibacter
|
MTFRFDNSYARDLEGFYVDWPAAPVPAPRLLRLNRPLAEELGLDPDLLEREGAEIFSGRRLPEGAHPLAQAYAGHQFGGFSPQLGDGRALLIGEITDRAGRRRDLQLKGSGRTPFSRGADGKAALGPVLREYLVGEAMHGLGIPTTRALAAVATGEPLLRQEGERPGAILTRVAASHIRVGTFQFFAARSDIDRVRRLADYAIARHYPELASAPEPYLAFYEAVAEAQAQLVARWMLVGFIHGVMNTDNMTISGETIDYGPCAFMEGYDPGTVFSSIDLQGRYAYGNQPYILAWNLARLGEALLPLLDGDPVRAADKATSVLETVGARYQGHWLAGMRAKLGLAGAEEGDARLAEDLLEAMRSQRADWTLTFRRLAEAVTDEGALRPLFRDPAALAGWLPRWRARLAPDAAERMRATNPIYIARNHRVEEALAAAHAGDLAPFDRLLEALADPFTERADRELFALPAPEGFDDSYRTFCGT
|
Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
|
Q3J3V1
|
Q06SJ6
|
PSBC_STIHE
|
Protein CP-43
|
Stigeoclonium
|
METLYNGTLSLGGKDQESTGFAWWSGNARLINLSGRLLGAHVAHAGLIVFWAGAMNLFEVAHFVPEKPMYEQGLILLPHLASLGYGVGPGGEVIDTFPYFVSGVLHLISSAVLGFGGVYHSLIGPETLEETFPFFGYTWKDKNKMTSILGFHLIILGFGAWLLVWKAMYFGGVYDTWAPGGGDTRIITNPTTNPAVIFGYLLKSPFGGDGWIVSVDNMEDIIGGHIWIGTLEIFGGIWHIFTQPWAWTRRAFVWSGEAYLSYSLGAIALMGFVACCMGWFNNTAYPSEFYGPTGPEASQSQAFTFLVRDQRLGANVASAQGPTGLGKYLMRSPTGEIIFGGETMRFWDFRGPWLEPLRGPNGLDLNKLKNDIQPWQERRAAEYMTHAPLGSLNSVGGVATEINSVNFVSPRSWLATSHFCLGFFFFVGHLWHAGRARAAAAGFEKGIDRLTEPVLSLKPLD
|
One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation.
|
Q06SJ6
|
O42499
|
NEUV_TAKRU
|
Neurophysin VT 1
|
Takifugu
|
MPQCALLLSLLGLLALSSACYIQNCPRGGKRALPETGIRQCMSCGPRDRGRCFGPNICCGEALGCLMGSPETARCAGENYLLTPCQAGGRPCGSEGGRCAVSGLCCNSESCAVDSDCLGETESLEPGDSSADSSPTELLLRLLHMSSRGQSEY
|
Vasotocin is probably an antidiuretic hormone.
|
O42499
|
Q7W3B3
|
DCUP_BORPA
|
Uroporphyrinogen decarboxylase
|
Bordetella
|
MSVAPLKNDVFLRALLREPVPYTPIWLMRQAGRYLPEYNATRARAGSFMGLAQNPDYACEVTLQPLARYPLDAAILFSDILTVPHAMGLGLDFAPGEGPRFAHPVRDESDVAKLAVPDMDSLRYVFDAVRTIRRELDGRVPLIGFAGSPWTIACYMVEGRGSDDYRLIKSMLYGRPDLLHRILEINAEATRHYLNAQIDAGAQAVMLFDSWGGVLADGLFQQFSLAYTRRVVEGLTREREGRRVPVIVFSKGGGQWLEEIAACGCDAVGLDWTVNLGTARRRVADAVALQGNLDPMTLFGGAQAVRAEARRTLDAFGPVGKGGHVFNLGHGISQYSPPEVVSELVDEVHTYSRALHAG
|
Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
|
Q7W3B3
|
Q18235
|
IFY1_CAEEL
|
Interactor of Fizzy protein
|
Caenorhabditis
|
MEDLNFEERGSTQIPASLQQHFSAKLGRQNELEKTPSRGGLGLVVNSSKTPGGKSLQSLASACKVPPSTKKNTIPIAFECYEDETDDQIADVATIKKTEKHPCSPIDTANRCETFDSLAADIEDDMLNLEDQDVVLSEDRPYGDVIDPAESEAEALAELGVEEWDSYPPIDPASRIGDDFNYVLRTEDFAEEGDVKLEETRHRTVIADIDEVKMSKAERNELFSMLADDLDSYDLLAEEANLPL
|
Acts as a chaperone and as an inhibitor for separase sep-1 . Plays an essential role in maintaining chromosome cohesion prior to meiotic and mitotic anaphase, in cytokinesis and in organizing the spindle and the centrosome . Ubiquitination-dependent degradation at the onset of anaphase is likely to activate sep-1 resulting in the proteolysis of the cohesin complex and the subsequent segregation of the chromosomes . Also required for cortical granule exocytosis .
|
Q18235
|
Q9BSG1
|
ZNF2_HUMAN
|
Zinc finger protein 661
|
Homo
|
MAAVSPTTRCQESVTFEDVAVVFTDEEWSRLVPIQRDLYKEVMLENYNSIVSLGLPVPQPDVIFQLKRGDKPWMVDLHGSEEREWPESVSLDWETKPEIHDASDKKSEGSLRECLGRQSPLCPKFEVHTPNGRMGTEKQSPSGETRKKSLSRDKGLRRRSALSREILTKERHQECSDCGKTFFDHSSLTRHQRTHTGEKPYDCRECGKAFSHRSSLSRHLMSHTGESPYECSVCSKAFFDRSSLTVHQRIHTGEKPFQCNECGKAFFDRSSLTRHQRIHTGESPYECHQCGKAFSQKSILTRHQLIHTGRKPYECNECGKAFYGVSSLNRHQKAHAGDPRYQCNECGKAFFDRSSLTQHQKIHTGDKPYECSECGKAFSQRCRLTRHQRVHTGEKPFECTVCGKVFSSKSSVIQHQRRYAKQGID
|
May be involved in transcriptional regulation.
|
Q9BSG1
|
Q4ICM9
|
PAM17_GIBZE
|
Presequence translocated-associated motor subunit PAM17, mitochondrial
|
Fusarium
|
MASPLKTFVLRMPATGLVRSSPKASFSTISAARPASCLSRSPFRKQCFKPAISINKSFSRAVSDKPQPETVQATPQPAPSNVLPPLDWNSFFKLRVKRRRYQMLFSITNGIFAGSGGAIFLSTGSAEPIISQIPLDPFMTLGLMTLAFSGLGWLSGPSVGNQVFYILNRQWKKQMTQKEAIFFERIKRNRVDPTNSSANNPVPDFYGEKISSVAGYRSWLKDQKAFNKKKTANFV
|
Component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner.
|
Q4ICM9
|
Q2SL32
|
RNC_HAHCH
|
Ribonuclease III
|
Hahella
|
MTAKLERLQRALGYTFKEPALLTLALTHRSFGGRNNERLEFLGDSVLNFIIADYLFGRFEEAREGQLSRLRARMVKGVTLAEIAREFDLGEYLRLGSGEMKSGGFRRESILADALESIIGAIYLDAGFEVCADRVLNWFEARLQKLNLKDTQKDSKTRLQEYLQARQLNLPRYEVISVQGEAHAQTFHVRCEIDGLSDATEGTGSSRRVAEQKAAKQALLALGVDQ
|
Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
|
Q2SL32
|
Q7VT71
|
MASZ_BORPE
|
Malate synthase G
|
Bordetella
|
MTERIPHHGLQVAASLHRFIEDEALSGSGLAPDEFWAGFAALVRDLAPRNRELLAERDRLQGEIDAWHRAHPGPVRDSAGYQALLERIGYLQPQPAQVTASTRDVDSEIASQAGPQLVVPVSNARYALNAANARWGSLYDALYGTDAIPPVAGDDGKGYNPARGEAVIARARAFLDEAAPLAQGSHADATAYAIEGGKLVVTLGAGQRTGLRNPAQLAGYQGDASQPAAVLLANNGLHFEIQIDRQHQIGATDAAGVKDVLLEAALTTIMDCEDSVAAVDADDKVLIYRNWLGLMKGDLSESVTKGGKTFTRRLNADRQYHKPDGGTLTLHGRSLMFVRNVGHLMTNPAILDEQGSEVPEGILDAVITSLAALPDRANRLNSRTGSIYIVKPKMHGPAEAAFANELFDRVEDLLKLPRHTIKMGIMDEERRTSVNLKACIAAAAARVAFINTGFLDRTGDEMHTGMEAGPMLRKGDMKSSAWITAYERNNVLVGLDCGLRGRAQIGKGMWAMPDMMAAMLEQKIGHPKAGANTAWVPSPTAATLHAMHYHQVDVAAVQQALEQTRYDSVRDELLAGLLTVPVGDPAAWSADDIQRELDNNAQGILGYVVRWIDQGVGCSKVPDINNVGLMEDRATLRISSQHIANWLRHGIVDRAQVNATFERMAKVVDQQNAGDPNYLPMAGHFDTSFAYRAACALVFEGLTQPNGYTEPLLHEYRQAFKAARR
|
Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA.
|
Q7VT71
|
Q0I8I3
|
HEM3_SYNS3
|
Pre-uroporphyrinogen synthase
|
unclassified Synechococcus
|
MALEHLRIASRRSQLAMVQTNWVKAELEKAHPGLAISVEAMATQGDKILDVALAKIGDKGLFTKELEAQMLVGRAEIAVHSLKDLPTNLPEGLMLGCITEREDPADALVVNSKNAEYTLETLPEGSIVGTSSLRRLAQLRYHYPHLQFKDVRGNVITRLEKLDSGNYDCLILAAAGLSRLGFGDRIHQSIPGNISLHAVGQGALGIECVCDRPEVMELIQVLNHAPTSARCLAERAFLRVLEGGCQVPIGVNTQIEGDTIQLTGMVASLDGKRLIRDEQAGPLADPEAVGRDLAHKLKDQGAGEILQEIFEMERGQ
|
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
|
Q0I8I3
|
P30657
|
PSB7_YEAST
|
Proteinase YSCE subunit PRE4
|
Saccharomyces
|
MNHDPFSWGRPADSTYGAYNTQIANAGASPMVNTQQPIVTGTSVISMKYDNGVIIAADNLGSYGSLLRFNGVERLIPVGDNTVVGISGDISDMQHIERLLKDLVTENAYDNPLADAEEALEPSYIFEYLATVMYQRRSKMNPLWNAIIVAGVQSNGDQFLRYVNLLGVTYSSPTLATGFGAHMANPLLRKVVDRESDIPKTTVQVAEEAIVNAMRVLYYRDARSSRNFSLAIIDKNTGLTFKKNLQVENMKWDFAKDIKGYGTQKI
|
Non-catalytic component of the proteasome which degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity. PRE3 and PRE4 are necessary for the peptidyl-glutamyl-peptide-hydrolyzing activity.
|
P30657
|
Q49ZF6
|
RL5_STAS1
|
50S ribosomal protein L5
|
Staphylococcus
|
MNRLKEKFNSEVTQNLVKQFDYSSVMEVPKIEKIVVNMGVGDAVQNTKVLDDAVEELQAITGQKPLITKAKKSVATFRLREGMPIGAKVTLRGERMYDFLDKLIAVSLPRVRDFQGVSKTAFDGRGNYTLGVKEQLIFPEIDYDRVNKVRGMDIVIVTTANTDEEARELLSQFGMPFHK
|
This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
|
Q49ZF6
|
B2UDL1
|
UNG_RALPJ
|
Uracil-DNA glycosylase
|
Ralstonia
|
MTRRANPAQAALFDEPAVDAADVSFIPLAQQFDALPADWKAVLTPCIAQTNWPELCAFVDGERAAGKPIFPTDVFRALHLTSVDDVRVVILGQDPYHGTGTVDGREIPQAHGLAFSVPAGVRVPPSLRNIYKEIEAEFGCKLPGTSGNLEGWAQQGVLLLNTVLTVEQGQAASHAKRGWERITDCLLEQLARVGHKRVFMLWGSHAQAKRALLSDGHLVLEAPHPSPLSAHRGFLGCGHFKTANDWLAAQRQPTIDWLKPQAA
|
Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
|
B2UDL1
|
B0TJA6
|
RS20_SHEHH
|
30S ribosomal protein S20
|
Shewanella
|
MANSKSAKKRALQSEKRRQHNASRSSMLRTYVKKVIAAINAGDHATATAAFAVAQPIVDRMATKGLIHKNKAARYKSRLNAKIKALVA
|
Binds directly to 16S ribosomal RNA.
|
B0TJA6
|
Q2RGI1
|
ACPS_MOOTA
|
4'-phosphopantetheinyl transferase AcpS
|
Moorella
|
MLEAGIDIIEISRLERSIKRHPRLLARVFTPAEVAYCLARHRPGASLAARFAAKEAVMKALGIGLGRCSWQDIEITREQGGRPRVILHNRARQLARELGVGEITVSLSHCHAYAAAVALVESSFSEEG
|
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
|
Q2RGI1
|
A5CQ58
|
ATPA_CLAM3
|
F-ATPase subunit alpha
|
Clavibacter
|
MAELSISPDEIRDALKDFVQSYEPGKASTTEVGYVLDAGDGIAHVQGLPGVMANELITFADGTLGLAQNLEESEIGVIVLGEFAGIEEGMEVRRTGEVLSVPVGDGYLGRVVDPLGNPIDGQGEIATEGRRALELQAPGVMQRKSVHEPMQTGIKAIDAMIPIGRGQRQLIIGDRQTGKTAIAIDTIINQKANWESGDTNKQVRCIYVAIGQKGSTIASVKGALEEAGAMEYTTIVASPASDPAGFKYLAPYTGSAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKLSDELGAGSMTGLPIIETKANDVSAYIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGGDAQVKSIKKVSGTLKLELAQYRSLEAFAIFASDLDAASRRQLARGARLTELLKQPQYSPFPIEEQVVSIWAGTKGKLDEVPVEDILRFERELLDHLHRNTEVLSQLKEKNVLTDDIVDAMDKAVDQFKLEFQTGEGKPLASVGSEKFEPAKAEDVNQEQIVKGKR
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
|
A5CQ58
|
Q95XR4
|
EPG2_CAEEL
|
Ectopic P granules protein 2
|
Caenorhabditis
|
MSANRTVTVFSSSAEDQEPIELAEDSLQNLDKMLAEEKEEHQLLKDEVVLLRKENVEAKTYSTLLEIMLDEAEEKASSAQETTSEENNLKILNRDLVAENLELKEMKEELRKIWLSDSKKFQEALTRISDENTKLQKDCHELESIRQCAQFALDNCNEELEKTQTENEEHESRIETLEREVCEKDIAMKDIVERKDEISLQLELQTKEFTSALNDLMYGREDTLKQIHQMKENWKVKQNEFEVEITKLKSQNDYFDSERLQLTDRIRALLNELSDVRLELGSTRLAMKEKAEVTEAVTSFNKDLRDKLEDEIARLGECLQFRKDEHEQDEAVIAHLEEQLKLGSDKAAAFSSEHSDTIELLRESETELMELRMENYDLKEDFKILKEEKEDVNRTCECLREQLSTTIQERDIEKGQMQSEMDAKMVAVHQQYAKQIDNMKYNHMLAINQELIKGQMALESGKKKHANEILTVRNELEQSNAAHQSLRDQCSLLLSSEDDLRTAHLALESKMTLVSEECIALRVSRANAQKEIGNLTEHHKLEVALLEDAKSGIQQRLHYATIEIEQLKKINEVTQAQFKKETDEKNAEINEFQAAMVSMKQQYNVLGNHCRVLTSQGISDRTTIDKLQETIREHTELAIETKRIHDAEIVQLNDAHKKLVDNLGVEELDEEPKASTESEEKAEWEMVDEE
|
Involved in autophagy . Thought to act as an adapter protein that brings PGL granules to autophagic structures containing lgg-1 . Association with other adapters such as sepa-1 is required for the accumulation and degradation of germ cell specific P-granules by autophagy in somatic cells . This ensures exclusive localization of the P-granules in germ cells . May also play a role in the removal of sepa-1 from somatic cells .
|
Q95XR4
|
Q99PF6
|
GAB1_MESAU
|
Growth factor receptor bound protein 2-associated protein 1
|
Mesocricetus
|
MSGGEVVCSGWLRKSPPEKKLKRYAWKRRWFVLRSGRLTGDPDVLEYYKNDHAKKPIRIIDLNLCQQVDAGLTFNKKEFENSYIFDINTIDRIFYLVADSEEDMNKWVRCICDICGFNPTEEDPVKPLGNSSQAPVDSPFAGNTAPASTQLEASPVTLPPSYQLISLPPHPDTLGLQDDPQDYLLLINCQSKKPEPTRTHADSAKPTSSETDCNDNVPSHKTPASSQSKHGVNGFFQQQMLYDCPPSRAASVSVDSSLYNLPRSYSHDVLPKESPSSTEADGQLYIFNTPSGTSSVEAQMRHVSISYDIPPTPGNTYQIPRTFPEGTLGQSSKLDTIPDIPPPRPPKPHLTHDRSPVETCGAPRTASDTDSSYCVPTAGMPPSRSNTISTVDLNKLWKDASSQDCYDIPRTFPSDRSSSLEGFHNQSKIKNVLTVASVSGEEPDENYVPMNPNSPPRQHSSSFTEPIQEPNYVPMTPGTFDFSSFGMQVPPPAHLGFRSSPKTPPRRPVPVADCEPPPVDRNLKPDRKAKPAPLEIKPLPEWEELQAPVRSPITRSFARDSSRFPLSPRPNSVHSTTSSSDSHDSEENYVPMNPNLSSEDPNLFGSNSLDGGSSSMIKPKGDKQVEYLDLDLDSGKSTPPRKQKNSGSGSSMADERVDYVVVDQQKTLALKSTREAWTDGRQSTESETPTKSVK
|
Adapter protein that plays a role in intracellular signaling cascades triggered by activated receptor-type kinases. Plays a role in FGFR1 signaling. Probably involved in signaling by the epidermal growth factor receptor (EGFR) and the insulin receptor (INSR). Involved in the MET/HGF-signaling pathway.
|
Q99PF6
|
Q9W603
|
SP16H_XENLA
|
Facilitates chromatin transcription complex subunit spt16
|
Xenopus
|
MAVTLDKEAYYRRIKRFFGSWKKGDDEFANVDAIVVSVGVDEEIVYAKSTALQTWLFGYELTDTIMVFCEEKILFMASKKKVEFLKQIANTKGNENANGTPAITLLVREKQNESNKGNFDKMIEAIKVSKKGKRIGVFIKDKFPGDFMKSWYDILNKESFEKVDISASVAYTIAVKEEGELNLMKKAASITSDVFSKFFKDRVMEIVDADEKVRHGKLAESVEKAIEDKKYLGGTDPSTIEMCYPPIIQSGGNYNLKFSVVSDKNHMHFGAITCALGIRYKSYCSNLVRTLMVDPTQEMQENYNFLLQLQEELLKELKHGAKICDAYQVIMDQVKKQKPDLMSKITKTLGFAMGIEFREGSLVINNKNQYKLKKGMVFSVHLGLAELNNKMGKKPEEKTYALFVGDTVLVNEEGAATVLTNVKKKVKNVGIFLKKEDEEEEEEEKDEAEDLLGRGSRAAALLTERTRNEMTAEEKRRTHQKELATQLNDEAKRRLTEQKGGQQTMKARKSNVSYKNASQVPKEPELREMKLYIDKKYETVIMPVFGISTPFHIATIKNISMSVEGDYTYLRINFFCPGSALGRNEGNIFPNPEATFVKEITYRASNVKTPGDPSVPSLNLQNAFRIIKEVQKRYKTREAEEKEKEGIVKQDSLVINLNRSNPKLKDLYIRPNIAQKRMQGSLEAHVNGFRFTSVRGDKVDILYNNIKHALFQPCDGEMIIVLHFHLKNAIMFGKKRHTDVQFYTEVGEITTDLGKHQHMHDRDDLYAEQLEREMRHKLKTAFKNFIEKVESLTKEDLEFEIPFRDLGFNGAPYRSTCLLQPTSSSLVNTTEWPPFVVTLDEVELVHFERVQFHLKNFDMVIVYKEYGKKVTMINAIPMASLDPIKEWLNSCDIKYTEGVQSLNWTKIMKTIVDDPEGFFEQGGWSFLEPDGEGSDAAEGDSESELDDETFNPSEDEEEEEEDSDEDYSDETEDSVDSEESADSEEESGKDWDELEEEARKADRESLYEEVEEQKSGNRKRKGHAPLPNPSKKRKK
|
Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II.
|
Q9W603
|
Q42609
|
PALY_BROFI
|
Phenylalanine ammonia-lyase
|
Bromheadia
|
MEVSKENGLCLQGRDPLNWGAAAAELQGSHLDEVKKMVEEFRRPVVKLEGVKLKISQVAAVAFGGGASAVELAESARAGVKASSDWVLESVDKGTDSYGVTTGFGATSHRRTKQGGALQKELIKFLNAGIFGSGNSNTLPSAATRAAMLVRINTLLQGYSGIRFEILKAIATLLNKNITPCLPLRGTITASGDLVPLSYLAGILTGRPNSKARTPNGSTVDATTAFRLAGISSGFFDLQPKEGLALVNGTAVGSGVASIVLFETNILAVMAELLSALFCEVMQGKPEFTDHLTHKLKHHPGQIEAAAVMEHILEGSSYMKMAKKLHEMDPLQKPKQDRYALRTSPQWLGPQIEVIRAATKSIEREINSVNDNPLIDVSRNKALHGGNFQGTPIGVSMDNTRLAIAAIGKLMFAQFSELVNDFYNNGLPSNLSSGRNPSLDYGFKGAEIAMASYCSELQALANPVTNHVQSAEQHNQDVNSLGLISSRKTAEAVDILKLMSTTFLVGLCQAVDLRHLEENLKNAVKNTVSQVAKRVLTMGVNGELHPSRFCEKDLIKVIDREYVFAYADDPCSSTYPLMQKLRAVIVEHALNNGVKEKDSNTSIFQKISSFENELKAALPKEVEAARAEFENGSPAIENRIKDCRSYPLYKFVKEVGSGFLTGEKVVSPGEEFDKVFNAICEGKAIDPMLDCLKEWNGAPLPIC
|
This is a key enzyme of plant metabolism catalyzing the first reaction in the biosynthesis from L-phenylalanine of a wide variety of natural products based on the phenylpropane skeleton.
|
Q42609
|
Q6LY53
|
THIM_METMP
|
4-methyl-5-beta-hydroxyethylthiazole kinase
|
Methanococcus
|
MDFVAKNLTKLRETNPLVQNITNYVVMNSTANSLLALGASPVMAHAMDELEEMVSIASALVVNIGTLDEYWIPSMEKAAKIASDLKKPIVLDPVGAGATKLRTKTALKILDFADISVLRGNFGEIAAVLGEHGKTRGVDSAAYDSNEAIELSKNAAKEFNTVSAVTGPVDHVSNGKEIYSISNGHSMLSKVTGTGCATTSIIGAFSAVDDPLKAAVSGLVVYGISAEMAFTEAPYPGTFQAKVYDWLYRIDEKLVLEKAKVNKFEI
|
Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
|
Q6LY53
|
A0A0A1I6E7
|
NDB4S_ANDCR
|
Antimicrobial peptide AcrAP1
|
Androctonus
|
MEIKYLLTVFLVLLIVSDHCQAFLFSLIPHAISGLISAFKGRRKRDLDGQIDRFRNFRKRDAELEELLSKLPIY
|
Has antimicrobial activity against the Gram-positive bacteria S.aureus (MIC=8 uM) and the yeast C.albicans (MIC=16 uM). Causes hemolysis on horse erythrocytes (64 uM for 100% hemolysis). Minimum bactericidal concentrations have also been tested against S.aureus and is four-fold higher (MBC=32 uM).
|
A0A0A1I6E7
|
B2GV47
|
RADX_RAT
|
RPA-related protein RADX
|
Rattus
|
MSGESDQPQPGPSHAGLYLEHRERDQAGVPGGVIRRAGSQRHRSWIQTVIEQITGSPRQCVTLSEVVPVSVLAVQRYLLEDEPRDTVPKPPLYCYDVTISDGVYQEKCYLDPSLNFLVYQNILKVGIEMRISRVSCLYNEKRLGQGILCIDKVHCGEPLDVISVETPFRNRAHEEKPERPLRGSKSHYLALWNNEDPYGDIWKTNKQPEEFNFNNTKIISLSHLEMTWHNRKNFPALLVRILHKSKLRYYGKPNKKMIEPYQTYLEVADSSGMVSVIMWNALCPEWYKSLRVGLILLLQDYSVKKSYPLRIQPDPVDPQMKLISTMEICLNLRDPPTNIVIIPEKQLKSEWKLPKLINRFITRSELDDMPENSICDVIGMLSFVGRVQRSKKKENSEDFWSYRWIHITDGTSEQPFIVQLFSTSQPEVFENIYPMTYFVCTQLKVVRNNSQVPKLLYLTTTNESRVLITGHRGQPYTYDTKAKKIIQWIKTKTNLEAKNTVIGGYYPYPPVPETFSKYSRFIKAESLLTTISEVRKVIEDLQYREQKRIAIQGIITAIKYIPYNHSAKSAPASETLQNASPPSTSQAAAKEGHYHERGSKRSQDDRPMDSLPMVLSLCAKRKILQGPTANPVPVPQPHSSAQMKGNKPNIPSRENSTANATGKSKRIINDRWESQLWRDKKFSLRDHLHYGHVDPESIPRKFILGHEKFLTQQFNSQPAKYVPPEGKPPKLDEFQSARSLGHFEVTILGLNHEIAIDVAFLPMYSPEDVETSQIDTFLTCMNYSCVYPPAAPVSGRVPDPKAVAGDIVKAAADLDRVHIIGILDICNLGNNKVEVCLQKIYTPE
|
Single-stranded DNA-binding protein recruited to replication forks to maintain genome stability. Prevents fork collapse by antagonizing the accumulation of RAD51 at forks to ensure the proper balance of fork remodeling and protection without interfering with the capacity of cells to complete homologous recombination of double-strand breaks.
|
B2GV47
|
Q8D4T9
|
NAGB_VIBVU
|
Glucosamine-6-phosphate isomerase
|
Vibrio
|
MRLIPLKTAAQVGKWAAAHIAKRINDFQPTAERPFVLGLPTGGTPLATYKALIELYQEGKVSFKHVVTFNMDEYVGISADHPESYRSFMYNNFFNHIDIQEENINLLNGNAEDHEAECQRYEDKIKSYGRINLFMGGVGNDGHIAFNEPASSLSSRTRIKTLTEDTRIANSRFFDGDINQVPKYALTIGVGTLLDSQEIMILVTGHNKALALEAAVEGSVNHLWTVSALQLHPKSVIVCDEPSTQELKVKTVKYFTELEAKNIVGF
|
Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
|
Q8D4T9
|
Q7YC63
|
CYB_APOMU
|
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
|
Apomys
|
MTNIRKTHPLIKIINHSFIDLPAPSNISSWWNFGSLLGLCLMIQIITGLFLAMHYTSDTTTAFSSVTHICRDVNYGWLIRYMHANGASMFFICLFIHIGRGMYYGSYTFMETWNIGVILLFAIMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFAFHFILPFIIAALVIVHLLFLHETGSNNPTGLNSNADKIPFHPYYTIKDLLGVFMLILFLMTLVLFFPDMLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALILSILILAFLPFLHTSKQRSLMFRPITQVLYWMLVANLLILTWIGGQPVEHPFIIIGQLASISYFSIILILMPISGIIEDKLLKWSL
|
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
|
Q7YC63
|
Q8YDR8
|
Y3107_BRUME
|
Probable ABC transporter permease protein BMEII0107
|
Brucella
|
MNARLTGLGLNLLSFAVGIGGWYLLTATGAVVLPGPVDVLERAVTLLLNGQLVGDIFASLRRVLSGFVLGVALAIPVGFLMGWYRIARSLIEPWVQFFRMIPPLAVIPLAIVTLGIDESPKIFVIFLASFLSSVVATYQGVISVDRTLINAARVLGAKDATIFARVIVPASVPFILVGVRIGLGSAWATVVAAELIAAQSGLGYRMQQAQLYYDLPTIFVSLVTIGILGLFMDRLLQAADRRLTQW
|
Probably part of an ABC transporter complex. Probably responsible for the translocation of the substrate across the membrane (Probable).
|
Q8YDR8
|
Q8HXE3
|
KMCP1_MACFA
|
Solute carrier family 25 member 30
|
Macaca
|
MSALNWKPFVYGGLASITAECGTFPIDLTKTRLQIQGQTNDAKFKEIRYRGMLHALVRIGREEGLKALYSGIAPAMLRQSSYGTIKIGTYQSLKRLFVERPEDETLLINVICGILSGVISSTIANPTDVLKIRMQAQSSTIQGGMIGNFMNIYQQEGTRGLWKGVSLTAQRAAIVVGVELPVYDITKKHLILSGLMGDTVYTHFLSSFTCGLAGALASNPVDVVRTRMMNQRVLQDGRCSGYTGTLDCLLQTWKNEGFFALYKGFWPNWLRLGPWNIILFVTYEQLKKLDL
|
Probable transporter.
|
Q8HXE3
|
A4WKJ7
|
GCH3_PYRAR
|
GTP cyclohydrolase III
|
Pyrobaculum
|
MHKVVLISLRGYREWTESLGPRREHIIQKVQARIHGALWSSFTAVGALPHHFRYDYLIALANNVPRHWIDTAVAKIRRSSPVEVDYCIGMGETPLDAYRSCGEHKEGKESNAVVAHVDIVNSTDATRINGPIHTYLRALDMLRTAAGACEDVGCIAFYLGGDNMVVYLPEPKAIYALLDRVEAPVRAGVGVSPRPYTAFVKATKGLDALRAENKTGVKVVR
|
Catalyzes the formation of 2-amino-5-formylamino-6-ribofuranosylamino-4(3H)-pyrimidinone ribonucleotide monophosphate and inorganic phosphate from GTP. Also has an independent pyrophosphate phosphohydrolase activity.
|
A4WKJ7
|
B2U822
|
RNPA_RALPJ
|
Protein C5
|
Ralstonia
|
MGLHAYPKAARLTKTDEFSSVFALRPVRRSRHFVLYVRANGDRPARLGVVIGKKFAKRAVERNLIKRQCRELFRLRQPLLGGRDVLIRLQAKFPRQDVPTVAAFKRICREELAQLFEVATRPLSAPPAATPPQPTAGSTP
|
RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
|
B2U822
|
Q8CPP8
|
QOX3_STAES
|
Quinol oxidase polypeptide III
|
Staphylococcus
|
MSHDANTIDSRTHEGELNKLGFWIFLTAEFALFGTLFATLLTLQHGGGYGGKLTTDLFELHLILIMTFALLISSYTCGIAIYYMRQEKQNLMMFWMIITVILGLVFVGFEIYEFAHYASEGVNPTIGSFWSSFFILLGTHGAHVSLGIVWVICLLIQIGTRGLDSYNAPKLFIVSLYWHFLDVVWVFIFTAVYMIGMVYSG
|
Catalyzes quinol oxidation with the concomitant reduction of oxygen to water.
|
Q8CPP8
|
Q8D3D5
|
OPGH_WIGBR
|
Glucans biosynthesis glucosyltransferase H
|
Wigglesworthia
|
MTNNKNYMKFLKFYNKKNKIKKIKNCSYKKLFCMNHYLRTGSNKRKKFLKKQYISTISVKKRLKCAWPKLINCSNFIIKDKKNIPLIKSYPKINRTSIAPTPWVIDSIFSFLKKFFFKKQNSKILSKNKKKKYLEKWEIVGIIRRYVFLILILSQTSIATYKLNSILPYKDISWSYTIYLFNKNIFLIIKYFSPYILQIFVLILFYILFFWVSASFWTAFMGFYQLITKKDEYNISNKSIVKEIKKNHRTAILMPICNEDVERVFAGLRATYESILSTGKIKFFDIYILSDSYNTDICMSEQKSWIDLCSETGFIGNIFYRRRNRRVKQKSGNIDDFCRRWGKNYSYMVILDADSIMSGKCLVKLVSLMESNPRAGIIQSIPKASGMNTLYARYHQFSTRVYGPLFTAGMHFWQLGESHYWGHNAIIRIKPFIKYCVLSPLPGNGIFSGSILSHDFVEAALMRRAGWSVWIAYDIPGSYEEPPPNLLDELKRDRRWCHGNLMNFRLFFMNGLHPVHRVVFLTGVMSYLSAPLWFAFLILSTILQIIYNIEFMCCFKINSYFYIIPYLHLEASIGLFFITLLLLLLPKFFSVILIISKNSIQYGGTRCFILSIILEIFLSMMFSPIKMMFHTFFIFRAFFGFSLSWKSPKRRDFSTSWKESIKSHIVQVVIGLIWSFLIIFFMTIKSLFIFFPIIFSLIISPLISVYSSYVKIGLIFKNFGLLLIPEEKYPPKEIINTKKYFKINKNKSLKNGFFQAILHPVYNALAVAMASSRHNSSILIDLNRKKFLDLILIKGLNKLNMIEKLTVLNDPIILTKLHFIYLLNNQ
|
Involved in the biosynthesis of osmoregulated periplasmic glucans (OPGs).
|
Q8D3D5
|
A6WRA3
|
TORD_SHEB8
|
Chaperone protein TorD
|
Shewanella
|
MSQVDINHARALVYQLLSSLFAREVDEQRLKELTSEAAQQFWEQLSLEAKLTQSVDKIRSTLNGIKDDETLLELAADYCGLFLVGTKHSASPYASLYLSGEDEPLLFGQQHQQMSEFLHQSKLQVQSHFPEPADHLAVMLAYMAHLCCHSEDSVQLSFLQTCVDSWLAKFINQLTQCDKNGFYSAVAILTLAWVKQDIAQLEPAEAVIS
|
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.
|
A6WRA3
|
Q0P5F9
|
AL8A1_BOVIN
|
Aldehyde dehydrogenase family 8 member A1
|
Bos
|
MAGRGGLLMLENFIGGKFLPCSSYLDSYDPSTGEVYCHVPNSGKEEIEAAVEAARAAFPGWSSRSPQERSQVLQRLADLLEQSLEELAQAESKDQGKTITLARTMDIPRAVHNFRFFASSILHHTSECTQMDHLGCLHYTVRAPVGIAALISPWNLPLYLLTWKIAPAIAAGNTVIAKPSELTSVTAWMMCRLLEKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERIMQLSAPHCKKLSLELGGKNPAVIFEDANLAECIPTTVRSSFANQGEICLCTSRIFVQRSIYSEFLKRFVEAARMWKVGIPSDPSADMGALISKAHLEKVRSYIKKARMEGAQILCGEGVDKLNLPPRNQAGYFMLPTVITDVKDESCCMKEEIFGPVTCVVPFDSEEEVIQRANNVKYGLAATVWSGNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGVGREGAKDSYEFFTEVKTITVKH
|
Catalyzes the NAD-dependent oxidation of 2-aminomuconic semialdehyde of the kynurenine metabolic pathway in L-tryptophan degradation.
|
Q0P5F9
|
Q5TIS6
|
NOTO_MOUSE
|
Homeobox protein notochord
|
Mus
|
MSSPAPSGTQVQPGSLRPCPGAVSPVVPRRLARGRLESSFSVEAILARPKTRELAATSLPLSTCTSLNLLGAVSQYGVLPWVCSTGSWLPAYLSVGVYPLCSMSCVPGLNVTHHQQGLRLTGSELPYCLGPLKWAPTVDLRDHGTERHTKRVRTTFNLQQLQELEKVFAKQHNLVGKERAQLAARLHLTENQVRIWFQNRRVKYQKQQKLKLPSSSVMEEPSSSSDGNIQSEDAELGIGS
|
Transcription factor that controls node morphogenesis . Acts downstream of both FOXA2 and Brachyury (T) during notochord development . Is essential for cilia formation in the posterior notochord (PNC) and for left-right patterning; acts upstream of FOXJ1 and RFX3 in this process and is required for the expression of various components important for axonemal assembly and function . Plays a role in regulating axial versus paraxial cell fate . Activates the transcription of ciliary proteins C11orf97 homolog, FAM183B and SPACA9 in the embryonic ventral node .
|
Q5TIS6
|
P47660
|
UVRA_MYCGE
|
Excinuclease ABC subunit A
|
Mycoplasma
|
MKPEWKNNDFIRVKGARENNLKNINIDIPKNQFVVITGLSGSGKSSLAFNTIYAEGRRRYLESLSSYARQFLGNSDKPDVDLIEGLSPAISIDQKTTSHNPRSTMGTVTEIYDYLRLLWARIGTPYCPNGHGSIQTQTINQIANQIFDLPNKSKVQLLAPTVKNQRGIFTNEFIKYKQLGFLRVLVDGQIYTLDDEIKLDKNTKHNISVVIDRIIINKDNQTYSRIVDSIETIDRLTNGKIEVLKEDGTILNFSKNHGCDKCGFSISELEPRLFSFNSPLGSCSYCKGLGFSYEPDVDKIIADSKLSINQGAIDIFKNIVHGTSLDWQRFLSLVNHYKIPLDKPIEQLDKSQLNLILEGSDEPIEIKTISNSGAKNIRFEHYEGIANLIKRRHLETNSQVSREWYSAYMSEITCKKCHGKKLIKDALSVKLGGIDIISFTELSIDKSIDFLLKLELNDEQKKIGELALKEIINRLSFLKNVGLDYLNLARRASTLSGGEAQRIRLATQIGSQLTGVLYVMDEPSIGLHQKDNMRLIKTMMVMRDLGNTLLVVEHDSETMLAADYLIDIGPKAGNEGGELVACGTPLQVMENSNSITGQYLSGKKQISIPKNRHSGNGKTIIIKGAKVNNLKNINVTIPLNKLVLITGVSGSGKSSLINQTLVPALERILYRKGVKKDTYKEIIGANNIDKIIVVSQDPIGRTPRSNPATYISVFDDIRDLFANTKEAKARGYTNSRFSFNVPGGRCDKCFGDGVIRIEMHFLPDVYVKCEVCNGKKYNSQTLEIKYLGKSIFDVLQMSCKEAYEFFKAIPNISRKLRLLCDVGLEYLQLGINVTFLSGGEAQRIKLSKFLQKKSTGKTLFVLDEPSTGLHLEDINKLLTIIQRIIKNGDTVVVIEHNLDIIKVADYIIDLGPEGGDNGGQIVAQGTPEQLINQVNKSYTAQYLSKILKPDSI
|
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate.
|
P47660
|
Q13DU3
|
RIMM_RHOPS
|
Ribosome maturation factor RimM
|
Rhodopseudomonas
|
MPAGLICIARIGAPHGVRGAMRLWSFTAEPLAVMDYGPLATKDGARSFEIATARPAKDHLVVTLKGVATREEAERLNGLELYVPRDRLPPTEDGEYYHADLIGLPAITPAGEPLGRVLAIHNFGAGDIIEIAPPQGATLLLPFTNAVVPTVDLTAGHVVIELPTEIEGDTPNHPEA
|
An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Probably interacts with S19. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
|
Q13DU3
|
Q2RH55
|
GLGA_MOOTA
|
Starch [bacterial glycogen] synthase
|
Moorella
|
MNKPLKILLVSPEVAPLAKTGGLADVAGSLPKALAAKGHEVRVAMPRYRQVKEVNYLTDLPVEMDGSLETAVIRQGKLPGEAGIPVYLIDNYKFFYRDGMYGYGDDAARFNFFCKAVLSMLPWLEFQPDIIHCNDWQTGPIPLFLKVKHEDNPFYRETATIYTIHNLQYQGTFPRNILKTMALSEEFFVPERLEFYGQVSYMKAGILYADLVNTVSKKYALEIQTPEYGERLDGLLRKRAADLRGILNGIDYEEFDPATDRRLAVNYDADHLEKKGENKAALQREMELPVRDVPVLGLISRLVSQKGLDLLAAILDPLMQQDLQFVLLGSGEDYYQQLFSRYKVKYRDKMAVKIGFDPVLAQHIYAGCDIFLMPSRFEPCGLGQMISLRYGAVPVVRATGGLEDTIKDLHQYPGVGNGFTFRDYQPQALLDTINRALHVYRHEPGEWRKLMRRGMAADFSWSASAGHYEEMYREALEKRRAAMFKVG
|
Synthesizes alpha-1,4-glucan chains using ADP-glucose.
|
Q2RH55
|
A2Z259
|
ZHD1_ORYSI
|
Zinc-finger homeodomain protein 1
|
Oryza sativa
|
MDFDDHDDGDEEMPPMPVSSSYETPPQHGLAGGGMAPKPPGEIGSHVKGPSCGGGRYRECLKNHAVGIGGHAVDGCGEFMAAGEEGTIDALRCAACNCHRNFHRKESESLAGEGSPFSPAAVVPYGATPHHQFSPYYRTPAGYLHHHQHHMAAAAAAAAAAAGGHPQRPLALPSTSHSGRDDGDDLSGMVGPMSAVGPLSGMSLGAGPSGSGSGKKRFRTKFTQEQKDKMLAFAERVGWRIQKHDEAAVQQFCDEVGVKRHVLKVWMHNNKHTLGKKLP
|
Putative transcription factor.
|
A2Z259
|
Q9RV39
|
AATNT_DEIRA
|
A-adding enzyme
|
Deinococcus
|
MFRRRPPLPPFPPGAALVGGAVRDWLRGVRSADYDWAHPDPAAGARALAALVGGAAFPLDEERGYWRVTAGEVQHDFVPLPPNLEDDLRRRDFTVNAIALREGRRLVDPLGGQQDLKRRVLRMVSEDNLRADPLRAWRAARFVTTLSFTLEPQTEQAVRQVAADLKAGRLPFPAWERVRDELHALLRSPDAARGILTLEALGLLDLTLPELREGQGLTQGGFHHLDVFEHGVEALHQLLTRRPDADLLLRWATLLHDVGKPRTFARDPDTGRRSFHGHDRVGAELTTQILTRLKLPGADVKRAAALVKAHMVQLPADDAQARRFVHRRRELLPDLLSLMLADREAARGPSSSELGRFAYMLAMERVLAALEEQPAAPPPLLSGKEVMALLGLTPGPRVGEVLRALAEARALGEVGTPQEARAFVQRWAEETPGS
|
tRNA nucleotidyltransferase involved in the synthesis of the tRNA CCA terminus. Adds the terminal adenosine residue to tRNA.
|
Q9RV39
|
A6QB69
|
PROB_SULNB
|
Gamma-glutamyl kinase
|
unclassified Sulfurovum
|
MKRIVIKVGSHVLTEDGSIARERMMALVELIADLKKHSYEVALVSSGAVAAGYTQLPLDRDDIANRQALAAIGQPLLLKMYQEKFARFDLLCSQVLFSADVFESDKHVSHAKVAIDTLLANNVVPIINENDTVSIEELVFGDNDRLSAHVAHYFDADLLVILSDIDALYDKDPNCFQDARRRAVVNEIEEEELAAEHTPNNEFATGGIVTKLQAADFLMKHGREMFLASGFELSDVKSFLIEGEHKGGTLFTSTKRS
|
Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
|
A6QB69
|
P72392
|
FABH1_STRCO
|
3-oxoacyl-[acyl-carrier-protein] synthase III 1
|
Streptomyces albidoflavus group
|
MSKIKPSKGAPYARILGVGGYRPTRVVPNEVILEKIDSSDEWIRSRSGIETRHWAGPEETVAAMSVEASGKALADAGIDASRIGAVVVSTVSHFSQTPAIATEIADRLGTDKAAAFDISAGCAGFGYGLTLAKGMVVEGSAEYVLVIGVERLSDLTDLEDRATAFLFGDGAGAVVVGPSQEPAIGPTVWGSEGDKAETIKQTVSWDRFRIGDVSELPLDSEGNVKFPAITQEGQAVFRWAVFEMAKVAQQALDAAGISPDDLDVFIPHQANVRIIDSMVKTLKLPEHVTVARDIRTTGNTSAASIPLAMERLLATGDARSGDTALVIGFGAGLVYAATVVTLP
|
Essential enzyme that catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain of fatty acids.
|
P72392
|
B1LWQ2
|
RS13_METRJ
|
30S ribosomal protein S13
|
Methylobacterium
|
MARIAGVNIPTNKRVVIALQYIHGIGAKKAEEITQKVNIPAERRVNQLTDAEVLQIRETIDRDYLVEGDLRREVSMNIKRLMDLGAYRGLRHRKQLPVRGQRTHTNARTRKGKAKPIAGKKK
|
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites.
|
B1LWQ2
|
Q09G14
|
RPOA_PLAOC
|
Plastid-encoded RNA polymerase subunit alpha
|
Platanus
|
MVREKVTVSTRTLQWKCVESRADSKRLYYGRFILSPLIKGQADTIGIAMRRALLGEIEGTCITRAKSEKIPHEYSTIVGIEESVHEILMNLKEIVLRSNLYGTRNASICIRGPGYVTAQDIISPPSVETVDNTQHIANLTEPIDFCIELEIERNRGYRMKTPNNSQDGSYPIDAVFMPVRNANHSIHSYANGNEKQEILFLEIWTNGSLTPKEALHEASRNLIDLFIPFLHAQEENILLEDNQNGVTLPFFTFHDRLAKIRKNEKEIALKYIFIDQSELPPRTYNCLKRSNIHTLLDLFNNSQEDLMKIEDFRIEDVKQILGILQKHFTVDLPKNKF
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
Q09G14
|
Q477Z0
|
ATPE_DECAR
|
F-ATPase epsilon subunit
|
Dechloromonas
|
MAMTVHCDVVSAEESIFSGLVEIAVFPGEAGELGILPRHTPLLTRIKPGTIRLKVPDQSEFELVYVSGGMLEVQPDMITVLADTAIRAHDLDEAKALEAKKRAEEALANRNAEMDYAAAEAELAQAVAQLQAIQRLRKHTH
|
Produces ATP from ADP in the presence of a proton gradient across the membrane.
|
Q477Z0
|
Q8MEY4
|
MATK_CERME
|
Intron maturase
|
Ceratozamia
|
MDKLQRDGKEDTSRQRRFLYLLLFQEDLYAIAYDHYFNRSSSFEPMENSSSNDRFSFLTVKRSISRIRQQNGSIIPFVNCDQNRLVGHSRSFYSELVLGGLTAVPEVPFSIRSKHSLEGMNEWTSFRSINSIFPLMEDKIPHSNFLLDIQIPHLTHPEILVRTFRRWIQDAPFLNLLRSVLHEHRNLTISSNLDQLILIASKENKRLSLFLWNYYAYECESLLVPLWKRFSHSRSLPYESFIERTPFYQKIKNIVIFYHKYIKKSLWFLKDPSIHYVKYRERSIIALRGTYLLVKKWRYHLTNFWQCHFHLWLQPYRIYIDEFSNNCFSLLGYLLSVKMKTSVVRIRMLDDSFITHLITKEFDPIAPTTLLIRSLAKERFCDISGHPISRLAWTGLTDDDILDRFDRIWRNIFHYHSGSSKKDGLYRMKYILRLPCAKTLACKHKSTIRVVRERFGSELFTKSFPKERESILLPFSKTRSQRERIWHSDIIQRNPLVNS
|
Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns.
|
Q8MEY4
|
A1KUN6
|
AROA_NEIMF
|
5-enolpyruvylshikimate-3-phosphate synthase
|
Neisseria
|
MTESVRLPVARLKPSTVALPGSKSISNRTLLLAALSDNACEIHSLLKSDDTDRMLEALDKLGVQIEYLAEDRLKVHGTGGRFPNRTADLFLGNAGTAFRPLTAALAVLGGDYHLHGVPRMHERPIGDLADALRIAGADVEYLGKEHYPPLHIGKRQDNGERVIPIKGNVSSQFLTALLMALPLTGQAFEIRMVGELISKPYIDITLKLMAQFGVQVANENYRVFKIPADAHYHAPEHLHVEGDASSASYFLAAGLIAATPVRVTGIGANSIQGDVAFARELEKIGADVVWGENFVEVSRPKERAVQSFDLDANHIPDAAMTLAIVALATGQTCTLRNIGSWRVKETDRIAAMANELRKLGAKVVEEAEAIHITPPKTLTPDAVIDTYDDHRMAMCFSLVSLLGVPVVINDPKCTHKTFPTYFDVFSSLTETTE
|
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
|
A1KUN6
|
Q5E7T0
|
FETP_ALIF1
|
Probable Fe(2+)-trafficking protein
|
Aliivibrio
|
MSRTVFCVRLNKEADGLDFQLYPGELGKRIFDNISKEAWGQWQHKQTMLINEKKLNMMDPEHRKLLETEMEGFLFDGKDVVIDGYTPPSE
|
Could be a mediator in iron transactions between iron acquisition and iron-requiring processes, such as synthesis and/or repair of Fe-S clusters in biosynthetic enzymes.
|
Q5E7T0
|
Q839F3
|
RL24_ENTFA
|
50S ribosomal protein L24
|
Enterococcus
|
MFVKKGDKVKVITGKDKNKEGVVLAAFPKQDKVIVEGVNVVKKHQKPNQAAPQGGILEVEAPIHVSNVMVIDPSNGEATKVAFKEVDGKKVRVSKKTGEVLDK
|
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
|
Q839F3
|
Q63DX8
|
LEU1_BACCZ
|
Alpha-isopropylmalate synthase
|
Bacillus cereus group
|
MKKILFMDTTLRDGEQSPGVNLNEQEKLQIARQLERLGIHVMEAGFAAASEGDFQSVKRIANTIQNATVMSLARAKESDIRRAYEAVKGAVSPRLHVFLATSDIHMKYKLCMSKEDVLDSIYRSVTLGKSLFPTVQFSAEDATRTARDFLAEAVEVAIRAGANVINIPDTVGYTNPEEYYSLFKYLQESVPSYEKAIFSCHCHDDLGMAVANSLAAVEGGALQVEGTINGIGERAGNAALEEVAVALHIRKDFYKAEPSMTLKEIKATSTLVSRLTGMVVPKNKAIVGANAFAHESGIHQDGVLKEVTTYEIIEPALVGESQNLFVLGKHSGRHAFTEKMKELGYEFTNDERDAVFEAFKKLADRKKEITEEDLRALMLGEAAFAAQQYNITQLQVHFVSNSTQCATVVLKDEEGNVFEDAATGSGSIEAIYNAIQRILGLECELADYRIQSITQGQDALAHVHVELKEGAHQVSGFGVAQDVLEASARAYVHAAGKLKSFIQLVK
|
Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
|
Q63DX8
|
A5DIR3
|
PLPL_PICGU
|
Patatin-like phospholipase domain-containing protein PGUG_03164
|
Meyerozyma
|
MTSSTPLYDENEDYIDENHINTFAKALLWEDDDHDGLASPPLPAYEGDKLAEVNAEELSSVLTPEPNNESEKSRPEFVVSHNDWYPINAPEKSKAKADAKGRKKRASTRDEFRSSAAYTLLRWPFLIIITVWILLLCILYTVVRAYVALSEYMLTWVGERKVLRNKLRASKTYEEWIENALELDRYLHLDKWSSIPRFSYYDYRTVKRTTSKLRMLRMRGMDEELMVFLQGCLKKNFAGIENRQLYAHRYYGTKNVVHVYIDEVVASIDHVTESENITPEDKRRFFRSVSRNYGRTALCLSGGACFAYTHFGIVKALLDNDLLPSIITGTSGGGLVAALACTRTDDELKQLLVPRLARKITACEDPWYVWIPRWWRTGARFDSTAWARKSNYFTLGSLTFQEAYHRTGRRLNISTVPADPHSPVILCNNITAPNCIIWSCLLASSAVPGILNPVVLMMKDSKKNTIVPFSLGSKWKDGSLRTDIPIDALKTYYNVNFTVVSQVNPHISLFFFAPKGSVGRPVASSRRKTRREKYASLRGGFIATALEHLFKLEIKKWLEMIKTLDLLPRLSESDWSSIWLQRFTGSITIWPRNNFRDFWYILSDPSEEGLGEMIRKGERYMFPKILFLKHRLSIENAIERGRTKSKLSTAHLEHSPRFSGTPEFAGPEFQLQTVHYDDDYDSESSAEETLSPGFSQGTHAVLTDESDDDSSDDEIDD
|
Probable lipid hydrolase.
|
A5DIR3
|
Q1LQG2
|
HLDD_CUPMC
|
ADP-L-glycero-beta-D-manno-heptose-6-epimerase
|
Cupriavidus
|
MTIIVTGAAGFIGSNIVKGLNERGETNIIAVDNLTRAEKFNNLVDCEIADYLDKTDFVARFARGDFGNVRAVFHEGACSDTMETDGRYMMENNYRYTLALLEACLEQGAQFLYASSAATYGASTMFREDRDYEKPLNVYGYSKFLFDQVVRRRLPSAHSQIVGFRYFNVYGPREFHKGRMASVAFHHFNQFRAEGTVKLFGEYNGYAPGTQSRDFVSVEDVVKVNLYFLDHPEKSGIFNLGTGRSQPFNDIAVSVVNALRESEGKPALSLDEMVQEGLVEYVKFPDALRGKYQCFTQSDVSRLRGAGYSDQFLTVQEGVSRYCKWLLERSA
|
Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose.
|
Q1LQG2
|
Q9U6L5
|
PEB1_DROME
|
PEB-me
|
Sophophora
|
MVRQLILVLSLILFCGSSHAVVSELARQSESAIQGLADIKMAPLRYLDVLFGGNPGGLRGLDGGNSASLSTLQAAKVANILARGDIASSGYSKISAGVGKGSDLITIIKNTRSYDPYLIPPGIPGYNYPLGWPLRYPLGPYWPNRPPWLPINSPPIRPGGLFPGGPSPGGPSPGEPSPGEPSPGGPSPGGPSPGGPSPGGPSPGGPSPGGPSPGGPFPGGSPPSPGGPLGPWQFPWILGGPRPNRPGRPFPGGILPGHLDGSVVPNSVLNVAGGIFGNGGLFGTGIFGQHGLFGTGFLSGPSLDPFGIFTPIGNFFGSLGNLFGFSSPSQIIPIFGGKFGPLGRGLQGSITLDVGGTVPSVKGILGQLLHPFLGFLG
|
Major protein component of the posterior mating plug. Accessory gland proteins constitute, or are required for formation of the anterior mating plug. Posterior mating plug forms before sperm transfer and the anterior mating plug is formed after the start of mating.
|
Q9U6L5
|
A4K2W7
|
WFDC5_AOTNA
|
WAP four-disulfide core domain protein 5
|
Aotus
|
MRIQSLLLLGALLAVGSQPPAAFGRKKGEKPGACPPDDGPCLLSVPDQCMEDRQCPLTRKCCYRACFRQCVPRVSVKLGSCPEDQLRCLSPMNHLCHKDADCSGKKRCCSSACGRDCRDPVRG
|
Putative acid-stable proteinase inhibitor.
|
A4K2W7
|
O13935
|
TRM4B_SCHPO
|
tRNA (cytosine-5-)-methyltransferase trm4b
|
Schizosaccharomyces
|
MGKRNKKVTQGKRAYNDKSEIVLENKQFEGYYKKQNLFRGKPNDEFDSFMEYMRKPLPTTFRICGYRHHAFELKNHFEKYYVPSLKNVVHEGQTIPPPTVLPWYPDGLAYIVDAQKDVIRKSPPLKRLQRFLVSENEAGNINRQEAVSMLPPLFLDVEPHHVILDMCAAPGSKTAQLIEAVYKKANIKDAAHDSKNLKSVEGLVIANDADPKRAQMLVHQINRLNSPNILVVNHDASTMPNIYVKGSSPSDGLNVIEEKKILKFDRILADVPCSGDGTFRKNLSLWREWSANSAFSLHPLQLRILIRGLQLLKVGGCLVYSTCSINPIENEAVVTAALKATGGAVSLVDVSKKLPLLKRDPGLLSWKVLDDSLNEFQSPAENTNDKIELTESMWPLPEEEMSKLHIERCARLYPHMQNTGGFFVAVLQKTDPINSRSFDPKKYTASMEILPPENKRQRTEKGVDEASNSTLTKSGNSYFDEEPFVYINPDDTSIKTIVDFYGIDPSFPRDQFFVRNQSGIPVRSIYFACSLFKEIIEANTNRVKFVHGGVRFFVKQEISQLLKDFSLKANKDICNFRIHSNGVNIISPFLNEKHFYDAGLKDLKILVKNEYPHVEQFSESGMLKKEFEKMPLGCNILRVDAQTKDGALMDMLILQPIWRSPTSCNLMLARKEKQNLSLELFGMDV
|
tRNA cytosine C(5)-methyltransferase that methylates cytosine to 5-methylcytosine (m5C) in tRNAs at position 49 and 50 . Trm4a and trm4b methylate different sets of tRNAs . Also methylates cytosine to m5C at positions (60, 61 and 62) in tRNA(Asp) .
|
O13935
|
B4UMK8
|
RNH_ANASK
|
Ribonuclease H
|
unclassified Anaeromyxobacter
|
MSQARFIAFSDGSALVNPGGPGGTGFVVLDRARPAYRFGGTRWVEDGPNAVTNNRMELRAVLEALEGLPGGEQVEVISDSRYVVDALSRWIHGWRKKGWRTASGEPVLNRDLIEALDARASALSVRYTWVRGHDGHAVNEVVDQLAQAAARGVAGPGEAEVVAALRAEAFLAGGPAAPRSSRA
|
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
|
B4UMK8
|
A1VYF1
|
GPMI_CAMJJ
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase
|
Campylobacter
|
MKQKCVLIITDGIGYNKNSKFNAFEAAKKPSYEKLFKEVPNSLLKTSGLAVGLPEGQMGNSEVGHMCIGSGRIIYQNLVRINKAIENKELEKNENLQKLLAKCKRVHIIGLYSDGGVHSMDTHFKAMLEICAKNGNEVFAHAITDGRDVNPKSGLNFIKDLKEFCENLGVHFATLCGRFYAMDRDKRWDRVKECYECLLGKAYKVPNLLEYLQKSYDENVTDEFIKAVQNENYKGMREEDGIIFINFRNDRMKQLVEVLNSKDFKEFEREKIFENLLTMSVYDDKFKLPVLFEKEKIENTLAQVISKAGLSQLHTAETEKYAHVTFFFNGGKEELLENETRVLIPSPKVKTYDEKPQMSAFEVCDAVKKGIEKGEDFIVVNFANGDMVGHTGDFNAAIKAVEAVDTCLGEIVECAKKHDYAFIITSDHGNCEAMQDEKGNLLTNHTTFDVFVFVQAKGVSKIKDNMGLSNIAASVLKILDLEIPKEMNEALF
|
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
|
A1VYF1
|
P56368
|
RK23_CHLVU
|
50S ribosomal protein L23, chloroplastic
|
Chlorella
|
MMLDLVKYPVIRTEKTTRLVENNQLSFDVDVRITKPQIRKIIEEFFNVKVLAVNTHRPPRKTNRLGSKPSYKRVIVTVDSDVTLLK
|
Binds to 23S rRNA.
|
P56368
|
Q830Q6
|
RL1_ENTFA
|
50S ribosomal protein L1
|
Enterococcus
|
MAKKSKKMQEALKKVDATKAYSVEEAVALAKDTNIAKFDATVEVAYKLNVDPKKADQQIRGAVVLPNGTGKTQTVLVFAKGEKAKEAEAAGADFVGDDDMVAKIQGGWFDFDVVVATPDMMATVGKLGRVLGPKGLMPNPKTGTVTMDVTKAVEEVKAGKVTYRVDKAGNIHVPIGKVSFDNEKLVENFNTINDVLLKAKPSTAKGQYIKNISVTTTFGPGIHVDQASF
|
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.
|
Q830Q6
|
Q8PFX6
|
QUEF_XANAC
|
PreQ(0) reductase
|
Xanthomonas
|
MNTPEDSTLGREVAYPSGYDPSLLFPIPRAAGRQAIGLTGDLPFIGRDRWHAYELSWLDAQGKPCVATATLHVPCDSPSLIESKSLKLYLNSLNATRFNSAEAVRTRIATDLSTRAGADVAVEFGLPPIDAVGEGESIDALDLSIDDYGPPNAAYLCAHAQPVVEEVLTSALLKSNCPVTGQPDWASVTLRYRGAPIDREGLLRYLVSFRDHAEFHEQCVERIFNDVLTQCAPQWLVVEARYTRRGGLDINPLRSSASVPTPLSIFRDLRQ
|
Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
|
Q8PFX6
|
Q9U4H5
|
AMX_DROME
|
TM2 domain-containing protein almondex
|
Sophophora
|
MRLQRQCIVVNMRSAIVLIMIFVLTGIRNSETASGGNQMDLSDSKGDHKDNSNASNGNGNANDNEVYVPPLVSSMVAKSGGGAGGLLDNITAYSSSSSSSSSNGNNNMLCPYDKETPCDRLQFPCIRCNYNHGCIYGRDLNVTCEVINNVQCLGERSFQRQMNCRYCYQTEMWQQSCGQRSSCNSATDKLFRTNCTVHHDVLCLGNRSFTRNLRCNWTQGYRWSTALLISLTLGGFGADRFYLGHWQEGIGKLFSFGGLGVWTIIDVLLISMHYLGPADGSLYI
|
Involved in the control of cell fates in the neurectoderm. Acts as a positive regulator of Notch pathway and is required at different levels during development.
|
Q9U4H5
|
B9FDT1
|
OST1B_ORYSJ
|
Ribophorin-1B
|
Oryza sativa
|
MAPSLSTAVSSLLLLLLLAAAISVSSSPPMPEDSIRVISAEKRIDLTSPIVKVFLTLKLENDATAPEASQVLLAFTPTEVEHLAIVKATRAEGKRKKKIYVPLSVKASDLAAAPNGARLYSILLSTPLKPAEVTTLEVFYALTHSLEPFPAEITQSDPQLVYYRDSAVLLSPYHVLEQVTYIKMPSNRVESFTRVDPTSRAGNEVKYGAYNNQLPNSYVPILVHYENNRPFAVVEEFVRKVEISHWGNVQITEQYKLKHGGAQHKGVFSRLEYQSRPSISGVSSFKNLLARLPPRVHSVYYRDEIGNISSSHLRSDSHKSELEIEPRYPLFGGWHCTFTIGYGLPLQDFLFESDDGRRYINLTFGCPLLDTVVDDLTIKVVLPEGSTSPQAVVPFLMEQYLETSYSYLDVVGRTTVVLKKRNVVGEHNVPFQVYYEFNPIFMLAEPLMLISAVFLFFVACIAYLHMDLSIGKS
|
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
|
B9FDT1
|
B8D867
|
RF3_BUCAT
|
Peptide chain release factor 3
|
Buchnera
|
MFDSNHEQELSKRRTFAIISHPDAGKTTITEKMLFFGKVIRVPGTIKGRGSGKYAKSDWMNIEKERGISITTSVMQFTYKNILMNLLDTPGHQDFSEDTYRILTAVDCCLVVIDAAKGIEERTRKLMDVARIHNTPIITFINKLDRDSRDPIEILDEIEKELKLHCIPISWPISCGKNFRGVYHIHDKIIHLYKSKFRKNFLTLDSFLDGSLNEYLGADLSIYIRQELELIMNVYSKFNKEKFLKGITTPIFFGSALGNFGIDHLLDSLIKWAPSPLYRQSNKRIIKPQERNFTGFIFKIQANMDLKHRDRIAFMRIVSGQYTKGMKLTHVRIKKNIIISDAFSFLAGERISINKAYPGDVIGLHNHGTIKIGDTFTQGEEIKFIGIPSFAPEIFRLIYLKNPLKQKQLKKGLVQLSEEGTVQVFRPILNNDLILGAIGILQFDVVIERLRIEYNIDAVYKKVNIVLARWINCGNHHSLYNLKKSYSSYLAYDISNSLIYLAPSSANLNIVMSQNSDISFNATREQ
|
Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP.
|
B8D867
|
A6QBQ7
|
KHSE_SULNB
|
Homoserine kinase
|
unclassified Sulfurovum
|
MLISVPATSANLGPGFDTLGLAVDLRNEIVIKPSKFLSLSTHGEGADNPKIKKNSLFLSIFNENYKRLSGKANNFRFEFTNRIPISRGLGSSSAVIVAALSGAYAMAGVKYNKREILNQALRYEHHPDNITPAVMGGFNVACVEGDRVYSKKRRMPDYLRAVVVVPNRTISTARSRTVLPKMYRKEETVYSLSRAAYMTALFMSESWDLLRIASKDKLHQARRMKMMPELFDVQKLALKQGALMSTLSGSGSTFFNLAYEKDTDRIAQSLRARFPQFRVFVLALDNNGVITK
|
Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
|
A6QBQ7
|
B5XP99
|
THIM_KLEP3
|
4-methyl-5-beta-hydroxyethylthiazole kinase
|
Klebsiella
|
MPELLNPAPVAHLRHLLRAHSPLVHCMTNDVVQTFTANVLLAVGASPAMVIDPREAAQFAAIADALLINVGTLTEDRAVAMRAAVEHARQAGKPWTLDPVAVGALTVRTAFCHELLALQPAAIRGNASEILALAGMSAGGRGVDTTDTAAAALPAAQALARRLATVVAVTGEVDYVTDGERVLSVAGGNPLMTRVVGTGCALSAVVAASAALPGDRLENVAAACGLMKQAGEIAARQGGPGSFIPAFLDALYQEVQG
|
Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
|
B5XP99
|
A8ZUH7
|
RUVB_DESOH
|
Holliday junction ATP-dependent DNA helicase RuvB
|
Desulfosudis
|
MKEKILTFSSDPSSPVTRHETEEDTGDDLFSLRPCDFEDYVGQDRTVETLRIAIAAAKQRSEPLEHVLFHGPPGLGKTTLAHIIAAEMGTSLTITSGPALEKGGDLIGMLTHLKRGDILFVDEIHRLPRTTEEFLYPAMEDFAVDFVFDKGIHARCHRYRLNQFVLVGATTRVGLLSAPLRDRFGIFRKFDFYSRQDLARIVSRSAALMGLTIDETCTMELARRSRGTPRIVNRLLKRVRDYVQVRHGGVITVSAIDDALALEGVDEKGLTGLDRSYLETIIQYYGGGPVGIEAIGATLQEETDTLVDVVEPFLLAEGLLQRTSSGRKATEAAYRHLGVQWRG
|
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.
|
A8ZUH7
|
P29933
|
COBS_SINSX
|
Hydrogenobyrinic acid a,c-diamide cobaltochelatase subunit CobS
|
Sinorhizobium
|
MMSKIDLDISNLPDTTISVREVFGIDTDLRVPAYSKGDAYVPDLDPDYLFDRETTLAILAGFAHNRRVMVSGYHGTGKSTHIEQVAARLNWPCVRVNLDSHVSRIDLVGKDAIVVKDGLQVTEFKDGILPWAYQHNVALVFDEYDAGRPDVMFVIQRVLESSGRLTLLDQSRVIRPHPAFRLFATANTVGLGDTTGLYHGTQQINQAQMDRWSIVTTLNYLPHDKEVDIVAAKVKGFTADKGRETVSKMVRVADLTRAAFINGDLSTVMSPRTVITWAENAHIFGDIAFAFRVTFLNKCDELERALVAEHYQRAFGIELKECAANIVLEATA
|
Catalyzes cobalt insertion in the corrin ring.
|
P29933
|
A4SLP3
|
NUOB_AERS4
|
NDH-1 subunit B
|
Aeromonas
|
MKYTLTRIDPDAPVERYPQEQSQTVDDPLAQDATRGIMMGRLEEVLQDTVNWGRKNSLWPYNFGISCCYVEMCTAFTSPHDVARFGAEVIRASPRQADFMVIAGTPFIKMAPVIQRLYEQLLEPKWVISMGACANSGGMYDIYSVVQGVDKFLPVDVYIPGCPPRPEAFLQALMLLQDSIGKERRPLSWVVGDQGIYRPDMPAEKDRKRGERIKVTNLRTPDEI
|
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
|
A4SLP3
|
A6UTT2
|
ADHS_META3
|
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase
|
Methanococcus
|
MKMFNNIKNTGKLIRLERIFDKKSEKTVIIPMDHGVSSGPVAGLKDMRTAINSVAEGGANSVLVHKGIVRHGHRGYGKDIGLIIHLSAGTGVSPDPNEKVIVTSVEEAIRMGADAVSVHVNMGAPTDCQMYQDLGKIAETCEYWGMPLIAMMYPRGEKITDEKDPEFVAHAARLGAELGADIIKTNYTGDIDSFKDVVKGCPAPIIIAGGAKSTDAEYLQMVKDSIEAGGAGVASGRNVFQHKDVIGITKATAMVVHENADVEEALKVIKK
|
Catalyzes a transaldol reaction between 6-deoxy-5-ketofructose 1-phosphate (DKFP) and L-aspartate semialdehyde (ASA) with an elimination of hydroxypyruvaldehyde phosphate to yield 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate (ADH). Plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids.
|
A6UTT2
|
Q0BXJ3
|
PURA_HYPNA
|
IMP--aspartate ligase
|
Hyphomonas
|
MAGVVVVGAQWGDEGKGKIVDWLSSRADVVVRFQGGHNAGHTLVIDGKVFKLALLPSGLVRGGKLSVIGNGVVVDPWHMLTEIEGIQAQGIEVSPESLVLADNASLILPWHKDIDAAREGALGAAQIGTTKRGIGPAYEDRVGRRAIRVADLADPAALDLKIERLLAHHRPLRAGLDLPEPDGAALKAALLEIAPQVLAYAQPVWKLLDEKVRRGSRILFEGAQGVMLDVDHGTYPFVTSSSVVAGNASAGSGVGPGAISYVLGLAKAYTTRVGAGPFPTEQDNDIGKRLGTVGHEFGTNTGRARRCGWFDSVMVRQACATSGVTGLALTKLDVLDGFEEIKICTAYKLNGKTIDYFPAGLTDQAAVEPVYETLKGWSGSTRGARSWTDLPPEAVVYVRRLEELVGKPCALVSTSPEREDVILMRDPFEG
|
Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
|
Q0BXJ3
|
B9L605
|
OBG_NAUPA
|
GTP-binding protein Obg
|
Nautilia
|
MFVDNIKLKVKSGKGGQGCVSFRREKFVVKGGPDGGDGGKGGDVIVECDKNTHTLSHYKGRKLLKAKNGRPGEGRKKHGANGEDLILKVPPGTVIKNAETGEVLLDMKEDGERKVLLEGGRGGLGNWHFRGPRNQTPRYAQPGEEGQELEIVLELKLIADVGLVGFPNAGKSTLISTLSNARPEIANYEFTTLTPKLGVVRVDEYRSFVMADIPGIIEGAHEGKGLGIEFLKHIERTSTILYMIDLSSYRDPVYQFKTLQKELKEYSEKLASRDYAIALTKCDSVEVEKIEEFFEKLGISKTEPKFKADPNLPCHFDDKTFVLPISSVANINIEALKFALFDLVEKNKRKENEENSF
|
An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
|
B9L605
|
Q9H7U1
|
CCSE2_HUMAN
|
Protein GCAP14 homolog
|
Homo
|
MEEKTQIKTFLGSKLPKYGTKSVRSTLQPMPNGTPVNLLGTSKNSNVKSYIKNNGSDCPSSHSFNWRKANKYQLCAQGVEEPNNTQNSHDKIIDPEKRVPTQGMFDKNGIKGGLKSVSLFTSKLAKPSTMFVSSTEELNQKSFSGPSNLGKFTKGTLLGRTSYSSINTPKSQLNGFYGNRSAGSMQRPRANSCATRSSSGESLAQSPDSSKSINCEKMVRSQSFSHSIQNSFLPPSSITRSHSFNRAVDLTKPYQNQQLSIRVPLRSSMLTRNSRQPEVLNGNEHLGYGFNRPYAAGGKKLALPNGPGVTSTLGYRMVHPSLLKSSRSPFSGTMTVDGNKNSPADTCVEEDATVLAKDRAANKDQELIENESYRTKNNQTMKHDAKMRYLSDDVDDISLSSLSSSDKNDLSEDFSDDFIDIEDSNRTRITPEEMSLKEEKHENGPPQDMFDSPKENEKAFSKTDEWIDISVSDRSECTKHTSGNNLVSPDTDYRAGSSFELSPSDSSDGTYMWDEEGLEPIGNVHPVGSYESSEMNSIDILNNLESCDLEDDDLMLDVDLPEDAPLENVECDNMNRFDRPDRNVRQPQEGFWKRPPQRWSGQEHYHLSHPDHYHHHGKSDLSRGSPYRESPLGHFESYGGMPFFQAQKMFVDVPENTVILDEMTLRHMVQDCTAVKTQLLKLKRLLHQHDGSGSLHDIQLSLPSSPEPEDGDKVYKNEDLLNEIKQLKDEIKKKDEKIQLLELQLATQHICHQKCKEEKCTYADKYTQTPWRRIPGGYSAPSFSPWQGSFQGIPRTVPPHRRQTSSTTAFQQPSQTHRSHPGKTNKATTYRGPQ
|
Microtubule-binding protein which might play a role in microtubule bundling.
|
Q9H7U1
|
Q61XH2
|
TIPIN_CAEBR
|
CSM3 homolog
|
Caenorhabditis
|
MDEMDDFFGNDELDREPSPFGEEAIEDNTGEEGSRRIIEPKLLRTKKLTNPRLALNEKTLTGPKGITALREAFQNFNPNPKDDPYKNLEKMMKKYAYWGHLMFPKMKTEDVLNRVETLGTRRQVKLYIMKQRLGESTDDVENEKRETKSKNGIIDDGADDDEDDLFNDLPEKETPTKPINHTEKVVDSPEKKNGQVSNNDAEEEEYRMMEEERLREEQEAREAEAEDELMEDFDLNNDW
|
Required for normal progression of S-phase. Important for cell survival after DNA damage or replication stress.
|
Q61XH2
|
O14653
|
GOSR2_HUMAN
|
Membrin
|
Homo
|
MDPLFQQTHKQVHEIQSCMGRLETADKQSVHIVENEIQASIDQIFSRLERLEILSSKEPPNKRQNARLRVDQLKYDVQHLQTALRNFQHRRHAREQQERQREELLSRTFTTNDSDTTIPMDESLQFNSSLQKVHNGMDDLILDGHNILDGLRTQRLTLKGTQKKILDIANMLGLSNTVMRLIEKRAFQDKYFMIGGMLLTCVVMFLVVQYLT
|
Involved in transport of proteins from the cis/medial-Golgi to the trans-Golgi network.
|
O14653
|
Q2GVL1
|
ATG8_CHAGB
|
Autophagy-related ubiquitin-like modifier ATG8
|
Chaetomium
|
MRSKFKDEHPFEKRKAEAERIRQKYADRIPVICEKVEKSDIATIDKKKYLVPSDLTVGQFVYVIRKRIKLSPEKAIFIFVDEVLPPTAALMSSIYEEHKDEDGFLYITYSGENTFGNFETA
|
Ubiquitin-like modifier involved in autophagosomes formation. With ATG4, mediates the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Participates also in membrane fusion events that take place in the early secretory pathway. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy.
|
Q2GVL1
|
A5VVJ8
|
HUTU_BRUO2
|
Imidazolonepropionate hydrolase
|
Brucella
|
MSNPRHNEREVRSPRGDELNAKSWLTEAPLRMLMNNLDPDVAERPHELVVYGGIGRAARTWDDFDRIVATLKTLNDDETLLVQSGKPVGVFRTHKDAPRVLIANSNLVPHWANWDHFNELDKKGLAMYGQMTAGSWIYIGAQGIVQGTYETFVEAGRQHYGGNLKGRWILTGGLGGMGGAQPLAAVMAGACCLAVECDETRADFRLRTRYVDEKTHSLDEALAKIDAWTKAGEAKSIALIGNAAEIFPELVKRGVKPDIVTDQTSAHDPVHGYLPLGWTVAEWRAKQENDPKAVEKAARASMKVQVQAMLDFWNAGIPTVDYGNNIRQMALEEGLENAFAFPGFVPAYIRPLFCRGIGPFRWAALSGDPEDIAKTDAKVKELLPDNKHLHNWLDMAKERIAFQGLPARICWVGLGDRHRLGLAFNEMVRNGELKAPIVIGRDHLDSGSVASPNRETEAMKDGSDAVSDWPLLNALLNTASGATWVSLHHGGGVGMGFSQHAGMVICCDGTEDADRRLERVLWNDPATGVMRHADAGYDIALDWARKQGLRLPAILGN
|
Catalyzes the conversion of urocanate to 4-imidazolone-5-propionate.
|
A5VVJ8
|
A4FZQ7
|
HIS3_METM5
|
Phosphoribosyl-AMP cyclohydrolase
|
Methanococcus
|
MDLDIKEIVKNMDLKFRNIEGKKLLLAISTDKSGKVLMTAFMSEESLEKSIETGFMHYYSTSRDKLWRKGEESGNVQKIINVFRDCDGDALLFTVEQTGWACHEGYMSCFHNKIDLSTGKSTVVGNKLD
|
Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
|
A4FZQ7
|
Q1J118
|
FOLD1_DEIGD
|
Methenyltetrahydrofolate cyclohydrolase
|
Deinococcus
|
MTKAQLFGKPLADDVTRGVRAALKEWAGAEPGFQPHLVSVLASEDEASRVYVHSKARQAERLGVRFTARDLGADAKQDELHAVLQALSADADVHGVVLELPLAPGLDADAALRHIAPCKDVEGLTPANLALIAAGREAEALLPPTPRSVRFLLREVLGDDLRGRRVAVIGPGRTVGRPLTFMLNNRGVTVTLCNECTRDLRDVLAPQDAVVVAVGHAGLLRPEQVQPHHVVIDAGINVTPGGVVGDAVPDLPVRAQTPVPGGVGPLTSALMYQNLVRAVKLQRGERVE
|
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
|
Q1J118
|
Q4R755
|
GPDM_MACFA
|
mtGPD
|
Macaca
|
MAFQKAVKGTILVGGGALATVLGLSQFAHYRRKQMNLAYVKAADYISEPVNREPPSREAQLLTLQNTSEFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRSTKLIHGGVRYLQKAIMKLDIEQYRMVKEALHERANLLEIAPHLSAPLPIVLPVYKWWQLPYYWVGIKLYDLVAGSNCLKSSYVLSKSRALEHFPMLQKDKLVGAIVYYDGQHNDARMNLAIALTAARYGAATANYMEVVSLLKKTDPQTGKVRVSGARCKDVLTGQEFDVRAKCVINATGPFTDSVRKMDDKDAAAICQPSAGVHIVMPGYYSPESMGLLDPATSDGRVIFFLPWQKMTIAGTTDTPTDVTPHPIPSEEDINFILNEVRNYLSCDVEVRRGDVLAAWSGIRPLVTDPKSADTQSISRNHVVDISESGLITIAGGKWTTYRSMAEDTINAAIKTHNLKAGPSRTVGLFLQGGKDWSPTLYIRLVQDYGLESEVAQHLAATYGDKAFEVAKMASVTGKRWPIVGVRLVSEFPYIEAEVKYGIKEYACTAVDMISRRTRLAFLNVQAAEEALPRIVELMGRELNWDDHKKQEQLETAKKFLYYEMGYKSRSEQLTDRSEISLLPSDIDRYKKRFHKFDADKKGFITIVDVQRVLESINVQMDENTLHEILNEVDLNKNGQVELNEFLQLMSAIQKGRVSGSRLAILMKTAEENLDRRVPIPVDRSCGGL
|
Calcium-responsive mitochondrial glycerol-3-phosphate dehydrogenase which seems to be a key component of the pancreatic beta-cell glucose-sensing device.
|
Q4R755
|
P41069
|
TRAV_ECOLI
|
Protein TraV
|
Escherichia
|
MKQTSFFIPLLGTLLLYGCAGTSTEFECNATTSDTCMTMEQANEKAKKLERSSEAKPVAASLPRLAEGNFRTMPVQTVTATTPSGSRPAVTAHPEQKLLAPRPLFTAAREVKTVVPVSSVTPVTPPRPLRTGEQTAALWIAPYIDNQDVYHQPSSVFFVIKPSAWGKPRIN
|
Involved in F pilus assembly. Appears to facilitate the polymerization of inner membrane-located pilin subunits into extracellular F pilus filaments.
|
P41069
|
Q02854
|
NUXM_NEUCR
|
Complex I-20.9kD
|
Neurospora
|
MSSTSSPTYTISKTLNTNYPLIDNDPHFRRVIGYARPSDYVHGTVAGAAGPGLLYLMEKMAPSGVGKGGFPKAMRLATAVGFFGGFLYFYQRSILRFYGMSENAREVQMDMREMVDKVKAGQPLYGVSTLPVDVQGMAARQSRYSALFFAVLPWFNFVNHNQHGVDTAKYYQQAERELEAERLGKGSSS
|
Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
|
Q02854
|
Q8R9I2
|
PSTB2_CALS4
|
Phosphate-transporting ATPase 2
|
Caldanaerobacter
|
MKKIEVRDLDLFYGEVQALKKINLDVEPNSVLALIGPSGCGKSTFIRTLNRMNDLIEGVKISGTVLLDGKDIYKEVDVIELRKKVGMVFQKPNPFPMTVYDNVAYGPRIHGIRDKRTLNEIVEKSLKAAALWDEVKDRLHHSALSLSGGQQQRLCIARTLAVEPEVILMDEPTSALDPISTMKIEELIEELKKKYTIIIVTHNMQQAGRVSDYTAFFLNGELVEWGPTDQVFYNPKDKRTEDYITGRFG
|
Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
|
Q8R9I2
|
Q4QM31
|
OBG_HAEI8
|
GTP-binding protein Obg
|
Haemophilus
|
MKFIDESLIRIEAGDGGNGCVSFRREKFIPKGGPDGGDGGDGGDVYLQADENLNTLIDYRFNKRFAAERGENGRSSDCTGRRGKDIILPVPVGTRAIDNDTKETLGDLTQHGQKMLVAKGGYHGLGNTRFKSSVNRAPRQKTMGTPGEKRDLLLELMLLADVGMLGLPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVVKVDDSHSFVVADIPGLIEGAADGAGLGIRFLKHLERCRVLIHLVDIAPIDGSNPADNVAIIESELFQYSEKLSEKPRWLVFNKIDTMSDEEAEERVREITEQLGWEEDYYLISAATRKNVPPLCRDIMDFIIANPREAETQQVAPEEVKFKWEDYHQEQLAGYQFDDDEDWDDDWTEEDDEGIEFIYKP
|
An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
|
Q4QM31
|
Q6ZGM7
|
YSL7_ORYSJ
|
Protein YELLOW STRIPE LIKE 7
|
Oryza sativa
|
MEPVNDFQEGISTEHAFEAEPVPSLSETITPRSMVVSFILSVTLSIVAMKVTLSSGFIPSFSIPAGLLGFCVSRASIRILDYFAVAQLPFTRQENTIIQTCVVACTSITFTGGFGTYILAMGKKAAVGDVNAQNNVEEPSFARMITFLFLISFAGMFIIMPFRKVMIIRHRLTFPSGTATAHLINSFHTPQGVKQARKQVTLLFKSFGGTIAWSLFQWFFASGPGCGFKFFPTFGLEAYKHGFFFDFTMANVGIGMMCPYMIVFSVFIGTIISCGVIWPYIESKEGIWYPSNLGPNSLNGIRGYKVFIGLSMIMADCLFVFLCIMVRTTCAMIKRRRQAMQGGGGNAQPFQGIDIADQPVKSFDDRRRAQVFLRDEIPDSVTIGCYVLLSIISIAAIPHLYPQMRYSHVALIYLAAPVFAFCNAYGFGVTDMNLASTYCKIAMFAFGSWVGIKSGGVVAALVAGGITMSILGNAADVAQDLKTGYLTLTSPRAVFISEAIGTALGCVVNPTVFWVFYRVYKMGSGDMGDMPYAKLYRGFAMLSVGDGEQGLPRHSMLLFKVFFVLALALSVFREVASRKEWRIRRYIPSTIGMAITFFMPPRVPVGMCIGSLVAYLWEKMDAGRGRMLSPALASGLICGDGVGSILLSMLTLMGARAPICIKFLSRGDNVKLDAFLATLHDMR
|
May be involved in the transport of nicotianamine-chelated metals.
|
Q6ZGM7
|
A1K5J4
|
MNMC_AZOSB
|
FAD-dependent cmnm(5)s(2)U34 oxidoreductase
|
Azoarcus
|
MPITPASLSFAEDGTPYSTAYGDVYHSSDGGLGQAHHVFLAGNGLPERWRGRERFVIVETGFGLGLNFLASWAAWRKDPQRSERLHFVSCELHPFRVEDLALLHARWPEFAPLAAELQANWPCLAPGVHRLHLDGGRVCLTLYFGDARDGLAQLDARADAFLLDGFSPAKNPDLWSARIFHLLARLAAADATLATWSVAGEVREGLRRAGFEVEKAPGFGGKRQMLRGRYLGRGHRPAPAAAERRALVIGAGVAGTSIAERLAARGWQVELLDAASGPAQGASGNHAGVLRPLPSLDDNRMGRLTRAGTLYGWRHIQRLQAAGLPLRAEACGVLHLARDAAQEAKMRAVVERLALPPAHLRFVSAAEASEIGGWPVPLGGWWFGDSGWVQPPSLCAANLSAGGEGIRAHWNARVTLARADTRWQARDAQGALLAEAPVAILAAGTGITGFPLAAPLPVVSARGQVSLLPAPAGSAPRVVMCRMGYVSPAVDGLRCAGATFDVGDDDATLRARDHHENLSKLEAMLPGYTAALATQPAEGRVGFRPASPDRLPMVGAVPALTTLAAPCALAEIPRHTGLYALSGFGARGLVWATLAAETLASQLDGEPLPLERDLVDALDPARFLLRPARTLRGED
|
Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34.
|
A1K5J4
|
P65598
|
ORN_MYCBO
|
Oligoribonuclease
|
Mycobacterium tuberculosis complex
|
MQDELVWIDCEMTGLDLGSDKLIEIAALVTDADLNILGDGVDVVMHADDAALSGMIDVVAEMHSRSGLIDEVKASTVDLATAEAMVLDYINEHVKQPKTAPLAGNSIATDRAFIARDMPTLDSFLHYRMIDVSSIKELCRRWYPRIYFGQPPKGLTHRALADIHESIRELRFYRRTAFVPQPGPSTSEIAAVVAELSDGAGAQEETDSAEAPQSG
|
3'-to-5' exoribonuclease specific for small oligoribonucleotides.
|
P65598
|
A8FCU5
|
CTAA_BACP2
|
Cytochrome aa3-controlling protein
|
Bacillus
|
MKFALRLLSVITTFVMLIVLIGGALVTKTGSGLGCGRQWPLCHGRFFPEMNPASIIEWSHRMSTGVSTILVLALAVLCWKKISPVFRETKFLVIMSIIFLLLQALLGALAVVFGSNALVMALHFGISLISFASVLLLALLVFEATRSETKLVKPLHIGKKMQFHIYGLITYTYIVVYTGAYVRHTKSSLACSVFPFCSKDGALPAYFNQWVQMSHRAAALLLFVWIFVAMFHAMKHYKEQKQLYYGWIISAILITLQAISGVMSVYSQLALGYALAHSFFISCLFGVLCYFCLLIARFKYESKEPFK
|
Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.
|
A8FCU5
|
Q9RXC9
|
ISPG_DEIRA
|
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase
|
Deinococcus
|
MSFDSLPALPLDPLPDAALPTAPRRRQTVSVNVGGVMVGSAHPIVVQSMTNTDTANAEATAIQVAQLARAGSEIVRVTVNTREAAAAVPELVQRLADIGVHVPIVGDFHYNGHLLLREYPETARLLAKYRINPGNVGAGQRHDENFATMIEVAKEFDKPVRIGVNWGSLDQQVLARLMDENAAAGHPKSPTDVTIDAMIVSALDSARFAEELGLGHDKILISVKVSSAPELWQVYRQLAPLCDYPLHLGLTEAGMGMKGIVASSVALAPLLTEGIGDTIRVSLTPEPGAPRKLEVEVAQQILQSLGLRQFLPQVTSCPGCGRTTSSFFQTLAQKIQDFIRESMPEWKAKYPGVEDMQVAVMGCVVNGPGESKHANIGISLPGTGEDPRAPVYQDGKLLTTLKGPRIAEEFQELLEKYVEERYGQGVAQG
|
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
|
Q9RXC9
|
Q9PNI7
|
CLPS_CAMJE
|
ATP-dependent Clp protease adapter protein ClpS
|
Campylobacter
|
MPKTQTLEQTKLSEPKMYKVILLNDDVTTMDFVIEILMNIFHQNLEKASQTMLEIHHNGSGICGIYTQEIALSKQKKVMDAAKLANFPLQAKVEEE
|
Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation.
|
Q9PNI7
|
Q9W799
|
CPSF2_XENLA
|
Cleavage and polyadenylation specificity factor 100 kDa subunit
|
Xenopus
|
MTSIIKLTTLVGAQEESAVCYLLQVDEFRFLLDCGWDENFSMDIIDSVKKYVHQVDAVLLSHPDPLHLGALPYAVGKLGLNCAIYATIPVYKMGQMFMYDLYQSRHNTEDFSLFSLDDVDCAFDKIQQLKYNQIVHLKGKGHGLSITPLPAGHMIGGTIWKIVKDGEEEIVYAVDFNHKREIHLNGCSLEMINRPSLLITDSFNATYVQPRRKQRDEQLLTNVLETLRGDGNVLIAVDTAGRVLELAQLLDQIWRTKDAGLGVYSLALLNNVSYNVVEFSKSQVEWMSDKLMRCFEDKRNNPFQFRHLTLCHGYSDLARVPSPKVVLASQPDLECGFSRELFIQWCQDPKNSVILTYRTTPGTLARFLIDHPSERIIDIELRKRVKLEGKELEEYVEKEKLKKEAAKKLEQSKEADLDSSDDSDVEEDIDQITSHKAKHDLMMKNEGSRKGSFFKQAKKSYPMFPAPEDRIKWDEYGEIIKPEDFLVPELQVTEDEKTKLESGLTNGDEPMDQDLSDVPTKCVSTTESMEIKARVTYIDYEGRSDGDSIKKIINQMKPRQLIIVHGPPDATQDLAEACRAFGGKDIKVYTPKLHETVDATSETHIYQVRLKDSLVSSLKFCKAKDTELAWIDGVLDMRVSKVDTGVILEERELKDEGEDMEMQVDTQVMDASTIAQQKVIKSLFGDDDKEFSEESEIIPTLEPLPSNEVPGHQSVFMNEPRLSDFKQVLLREGIHAEFVGGVLVCNNMVAVRRTETGRIGLEGCLCEDFFKIRELLYEQYAIV
|
CPSF plays a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. In X.laevis this subunit seems to be predominantly involved in cytoplasmic polyadenylation reaction. May also be involved in the histone 3'-end pre-mRNA processing.
|
Q9W799
|
Subsets and Splits
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