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
|
|---|---|---|---|---|---|---|
Q7VC50
|
PCBG_PROMA
|
Divinyl chlorophyll a/b light-harvesting protein PcbG
|
Prochlorococcus
|
MQTYGDPNVSYAWYAANAGAVTNKSGRFISSHIAHTGLICFGAGANTLFELARYNPDLPMGSQGLVVLPHLAGLGLGGISNGVFTDTYQLLVVAILHLILSGVYGGGGMLHAFRYEEKLESYPATSRANKFKFDWNDPDRLTFILGHHLLFLAAGNIQFVEWARVHGIYDPVAGAVRQVEYNLDLGMIWNHQFDFLSISSLEDIMGGHAFLAFFMAAGGVFHILTKNYGEYNSFKGADLLSAEFVLSTSLAGAAYTAFVAALWCASNTTIYPVDLYGDVLQFKLGIAPYWIDTDSSLAADAHTGRAWLTNVHFFIGFFYLQGHFFHGLRALGFDFKSIGKLFDNLETSETTLN
|
The antenna complex functions as a light receptor, it captures and delivers excitation energy to photosystems I. The Prochlorales pcb genes are not related to higher plant LHCs.
|
Q7VC50
|
B6DD45
|
TXF12_LYCSI
|
Toxin-like structure LSTX-N12
|
Lycosa
|
MNSKIFAVLLLLAFLSCVLSDQYCPKSSITACKKMNIRNDCCKDDDCTGGSWCCATPCGNICKYPTDRPGGKRAAGGKSCKTGYVY
|
Has antibacterial activity.
|
B6DD45
|
Q42997
|
NIR_ORYSJ
|
Ferredoxin--nitrite reductase, chloroplastic
|
Oryza sativa
|
MASSASLQRFLPPYPHAAASRCRPPGVRARPVQSSTVSAPSSSTPAADEAVSAERLEPRVEQREGRYWVLKEKYRTGLNPQEKVKLGKEPMSLFMEGGIKELAKMPMEEIEADKLSKEDIDVRLKWLGLFHRRKHQYGRFMMRLKLPNGVTTSEQTRYLASVIEAYGKEGCADVTTRQNWQIRGVTLPDVPAILDGLNAVGLTSLQSGMDNVRNPVGNPLAGIDPDEIVDTRSYTNLLSSYITSNFQGNPTITNLPRKWNVCVIGSHDLYEHPHINDLAYMPAVKGGKFGFNLLVGGFISPKRWEEALPLDAWVPGDDIIPVCKAVLEAYRDLGTRGNRQKTRMMWLIDELGMEAFRSEVEKRMPNGVLERAAPEDLIDKKWQRRDYLGVHPQKQEGMSYVGLHVPVGRVQAADMFELARLADEYGSGELRLTVEQNIVIPNVKNEKVEALLSEPLLQKFSPQPSLLLKGLVACTGNQFCGQAIIETKQRALLVTSQVEKLVSVPRAVRMHWTGCPNSCGQVQVADIGFMGCLTKDSAGKIVEAADIFVGGRVGSDSHLAGAYKKSVPCDELAPIVADILVERFGAVRREREEDEE
|
Catalyzes the six-electron reduction of nitrite to ammonium.
|
Q42997
|
Q9EXU8
|
PQQE_RHIME
|
Pyrroloquinoline quinone biosynthesis protein E
|
Sinorhizobium
|
MSDTIARPAETARTLPRILPPMAMLAELTHRCPLACPYCSNPIALTQAKEELSTEEWTGVFAQAADLGVLHLHLSGGEPAARRDLVELTQAASSLGLYTNLITSGVGLTEARMNSLADAGLDHIQLSIQGVSPESADRIGGYKGGYERKMAVAGWAADAAIPLTLNAVCHRQNMGEIDEMIELAIRLKARRIEVATVQFHGWAERNKEVLMPTREQVECATRTVAEAREKYQGILVIDYVPADYYSKYPKACMGGWGRVGLNVTPSGRVLPCHAAETIPSLSFENVRENSLSSIWYESNAFNAYRGEDWMPELCRSCERKKVDFGGCRCQAMALAGDASATDPVCIRSPLRDRLTLEVEQLSAPSVVPMNYRGRA
|
Catalyzes the cross-linking of a glutamate residue and a tyrosine residue in the PqqA protein as part of the biosynthesis of pyrroloquinoline quinone (PQQ).
|
Q9EXU8
|
O25728
|
HCPC_HELPY
|
Cysteine-rich protein C
|
Helicobacter
|
MLENVKKSFFRVLCLGALCLGGLMAEQDPKELVGLGAKSYKEKDFTQAKKYFEKACDLKENSGCFNLGVLYYQGQGVEKNLKKAASFYAKACDLNYSNGCHLLGNLYYSGQGVSQNTNKALQYYSKACDLKYAEGCASLGGIYHDGKVVTRDFKKAVEYFTKACDLNDGDGCTILGSLYDAGRGTPKDLKKALASYDKACDLKDSPGCFNAGNMYHHGEGATKNFKEALARYSKACELENGGGCFNLGAMQYNGEGVTRNEKQAIENFKKGCKLGAKGACDILKQLKIKV
|
May hydrolyze 6-aminopenicillinic acid and 7-aminocephalosporanic acid (ACA) derivatives.
|
O25728
|
C6HFQ7
|
SHO1_AJECH
|
Osmosensor SHO1
|
Histoplasma
|
MVTYSANYSTSFQKRSPFAVHNRRSNMARMDFNNIVGDPFALITISTSLIAWLLSFATCVISDIQGAFPNFAWWAVGYMLCAIIGISLVLASQTSHVYGVAIVGYLAAGLTFTTLAVNSLIYDDQASKQAGAAGFILQSMVTIVWIFYFGSSSQTSSRPYLDSMGAGKEHPSYRNSKPLSTNYGARPETVVSGNQPPQMYTSAQLNGFETSSPVSGYPPTAANGAENGTQNRFVGPAIGSQSNLGGGSTLGADHPSTPNEVSQPTVYPYRAKAIYSYEANPDDANEISFSKHEILDVSDVSGRWWQAKKASGETGIAPSNYLILI
|
Plasma membrane osmosensor that activates the high osmolarity glycerol (HOG) MAPK signaling pathway in response to high osmolarity.
|
C6HFQ7
|
P25166
|
EF1A_STYLE
|
Elongation factor 1-alpha
|
Stylonychia
|
MPKEKNHLNLVVIGHVDSGKSTSTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDIALWNFETAKSVFTIIDAPGHRDFIKNMITGTSQADAAILIIASGQGEFEAGISKEGQTREHALLAFTMGVKQMIVAVNKMDDKSVNWDQGRFIEIKKELSDYLKKIWLQPRQDPFIPISGWHGDNMLEKSPNMPWFTGSTLIDALDALDQPKRPKDKPLRLPLQDVYKIGGIGTVPVGRVETGLLKPGMVLTFAPMNITTECKSVEMHHESLTEAEPGDNVGFTVKNLSVKDLRRGYVASDSKNDPAKDTTNFLAQVIVLNHPGQIQKGYAPVLDCHTAHIACKFDEIESKVDRRSGKVLEEEPKFIKSGEAALVRMVPQKPMCVEAFNQYPPLGRFAVRDMKQTVAVGVIKEVVKKEQKGMVTKAAQKKK
|
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
|
P25166
|
P22612
|
KAPCG_HUMAN
|
cAMP-dependent protein kinase catalytic subunit gamma
|
Homo
|
MGNAPAKKDTEQEESVNEFLAKARGDFLYRWGNPAQNTASSDQFERLRTLGMGSFGRVMLVRHQETGGHYAMKILNKQKVVKMKQVEHILNEKRILQAIDFPFLVKLQFSFKDNSYLYLVMEYVPGGEMFSRLQRVGRFSEPHACFYAAQVVLAVQYLHSLDLIHRDLKPENLLIDQQGYLQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAVGFPPFYADQPIQIYEKIVSGRVRFPSKLSSDLKHLLRSLLQVDLTKRFGNLRNGVGDIKNHKWFATTSWIAIYEKKVEAPFIPKYTGPGDASNFDDYEEEELRISINEKCAKEFSEF
|
Phosphorylates a large number of substrates in the cytoplasm and the nucleus.
|
P22612
|
Q04881
|
OPA68_NEIGO
|
opA27.5
|
Neisseria
|
AGEGNGRGPYVQADLAYAYEHITHDYPKPTDPSKGKLSTVSDYFRNIRTHSIHPRVSVGYDFGGWRIAADYARYRKWNDSKYSVSIKNLQRRTSNGNRRDRKTENQENGSFHAVSSLGLSAVYDFKLNDKFKPYIGARVAYGHVRHSIDSTKKITQFLTTAGARGTVSTVHPPYKSTQDAHHQSDSIRRVGLGVIAGVGFGITPKLTLDAGYRYHNWGRLENTRFKTHEASLGVRYRF
|
Implicated in a number of adherence functions. OPA proteins are implicated in pathogenesis and are subject to phase variation.
|
Q04881
|
Q2U6A1
|
DNLI4_ASPOR
|
Polydeoxyribonucleotide synthase [ATP] 4
|
Aspergillus subgen. Circumdati
|
MDSDDDYNGPADTNPRLEDEESDLDEKYPNRPRNHSTTLPFHVLFQTLFYPLSEIKKKPAGPARKKVGPHGLSSVNLTPLEKRRDIIDRFISRWRKEVGDDIYPAFRLILPDKDRDRAMYGMKEKAIGKLLIRIMKIDKNSEDALNLLNWKLPGQTTTSSMAGDFAGRCFGVLSKRPMRTEVGDMTIEEVNEKLDHLSAASKENQQLPILTEFYRRMNPEELMWLIRIILRQMKVGATERTFFDVFHPDAENLYSISSSLRRVCWELHDPNIRLEAEDRGITLMQCFQPQLAQFQMHSLDRMISRMRLTEDDPVFWIEEKLDGERMQLHMDSNDSVPGGRTFRFWSRKAKDYTYLYGNGIQDENGALTRYLSDAFADGVESLILDGEMITWDTEQDAIAPFGTLKTAALSEQRNPYSSTTRPLFRIFDILYLNGRDLTRYTLRDRRNALQKSIKPVYRRFEIHPYEEATGKTEIEEALRRVVEEASEGLVLKNPRSPYRLNERHDDWMKVKPEYMTEFGESLDVVVIGGYYGSGHRGGGLSSFLCGLRVDDAHSSQGMVASKCYSFCKVGGGFTAADYANIRHHTDGKWHEWKSRKPPTTYIELAGGDAQYERPDMWIKPEDSVVLCVKAASVAVSDQFRIGLTLRFPRFKKLRMDKDWKSALSVQEFLDLKANAERERKEKEFNVDNSRKKRAKRDNKKPLAIVGYSAEAEAQYTGPSGNIFEGLNFYITTDSNTPVKKSKAELEQLVKANGGKFFQTSNAAPSTICIADRRTVKAASLQKSGNVNIIRPSWILDCIRQSEIDAGLPDSLLPLEPRHVFFATQDKKEEIAASVDRFNDSYARNTTNDELKEILKQMSKDHHFHASQNPKIVRKLNERIQEKVNAGWEMPSGWLFKGLTILFPQNDKVDDAEVDETSQTHQQYRLNLARNTVRFAGANVVDSKSSSVTHIVVAPGSSSSDVSSIRKSHSAKPGKKVPHLVTAEWIEECWKQRTLLGEEGFQPSRGT
|
Involved in ds DNA break repair. Has a role in non-homologous integration (NHI) pathways where it is required in the final step of non-homologous end-joining.
|
Q2U6A1
|
Q43767
|
NLT41_HORVU
|
CW-21
|
Hordeum
|
MARAAASQLVLVALVAAMLLVAADAAISCGQVSSALSPCISYARGNGAKPPAACCSGVKRLAGAAQSTADKQAACKCIKSAAGGLNAGKAAGIPSMCGVSVPYAISASVDCSKIR
|
Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues.
|
Q43767
|
Q9K4F6
|
DTD_STRCO
|
Gly-tRNA(Ala) deacylase
|
Streptomyces albidoflavus group
|
MRAVVQRVDGASVVVDGETVGAIDGEGLCVLVGVTHDDTKEKAAQLARKLWSVRILHDEKSCSDLDAPLLVISQFTLYGDARKGRRPTWNAAAPGDVAEPLVDEVVAQLRALGATVATGRFGAQMRVSLTNDGPFTVLVEV
|
An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality.
|
Q9K4F6
|
D2Y225
|
H2N01_CYRHA
|
Hainantoxin-II-14
|
Haplopelma
|
MKVTLIAILTCAAVLVLHTTAAEELEAESQLMEVGMPDTELAAVDEERLFECSVSCEIEKEGNKDYKKKKCKGGWKYKFNMCVKV
|
Postsynaptic neurotoxin.
|
D2Y225
|
O53585
|
GLFT2_MYCTU
|
Polymerizing galactofuranosyltransferase GlfT2
|
Mycobacterium tuberculosis complex
|
MSELAASLLSRVILPRPGEPLDVRKLYLEESTTNARRAHAPTRTSLQIGAESEVSFATYFNAFPASYWRRWTTCKSVVLRVQVTGAGRVDVYRTKATGARIFVEGHDFTGTEDQPAAVETEVVLQPFEDGGWVWFDITTDTAVTLHSGGWYATSPAPGTANIAVGIPTFNRPADCVNALRELTADPLVDQVIGAVIVPDQGERKVRDHPDFPAAAARLGSRLSIHDQPNLGGSGGYSRVMYEALKNTDCQQILFMDDDIRLEPDSILRVLAMHRFAKAPMLVGGQMLNLQEPSHLHIMGEVVDRSIFMWTAAPHAEYDHDFAEYPLNDNNSRSKLLHRRIDVDYNGWWTCMIPRQVAEELGQPLPLFIKWDDADYGLRAAEHGYPTVTLPGAAIWHMAWSDKDDAIDWQAYFHLRNRLVVAAMHWDGPKAQVIGLVRSHLKATLKHLACLEYSTVAIQNKAIDDFLAGPEHIFSILESALPQVHRIRKSYPDAVVLPAASELPPPLHKNKAMKPPVNPLVIGYRLARGIMHNLTAANPQHHRRPEFNVPTQDARWFLLCTVDGATVTTADGCGVVYRQRDRAKMFALLWQSLRRQRQLLKRFEEMRRIYRDALPTLSSKQKWETALLPAANQEPEHG
|
Involved in the galactan polymerization of the arabinogalactan (AG) region of the mycolylarabinogalactan-peptidoglycan (mAGP) complex, an essential component of the mycobacteria cell wall. Thus, successively transfers approximately 28 galactofuranosyl (Galf) residues from UDP-galactofuranose (UDP-Galf) onto the galactofuranosyl-galactofuranosyl-rhamnosyl-GlcNAc-diphospho-decaprenol (Galf-Galf-Rha-GlcNAc-PP-C50) acceptor produced by GlfT1, with alternating 1->5 and 1->6 links, forming a galactan domain with approximately 30 galactofuranosyl residues.
|
O53585
|
Q10279
|
FUR4_SCHPO
|
Uracil permease
|
Schizosaccharomyces
|
MESVDNNSFFSRIRNSNAYRKVKDFVILDHRPGMTMAERMLTNKDLYPVPPSKRLWGPWNFISFWLADAVNINTWMISATAIELGLNWWEAWICVWVGYLICGILVATTGRPGAVYHISFPVLSRSSFGTWGSLWPILNRSVLACVWYGVQAWIGGECVVLMIRSIWPSFSHIPNTMAKSGTETYQWVGFFIFWLLSNIAIWFPVHQIRHLFTFKAIVAPPAAIAFLIWALVKAHGAGPVIHEPTKLGQYEHAWVVINGIVTCIDGFATLIVNNPDFARFATTPGAVHWPQIITVPLAFGVTSLIGVLVSSASKAIYGTTLWDPTQLLASFLDHSNAHGVRAGVFFIAFGLCIAQLGVNIAANSVSAGNDLSALLPTVINVRRGGYIASIIALCMCPWNLLSSNNNFTTYLSSYSVFLSSFAGVIIADYYFVRKGLIRVAPLYSSSSSSPYYFWKGINFRAFASYICGMLINIVGMAGSTGQKVPKVANTMFNLNYFLGITVACLSHIIICKIFPVTECGEKMLSEVPEEADDYLLTLASEDSIDKDSTSEIYIDGLPTEKEVEKDDVLSITSKKLSGCFP
|
Transport of uracil.
|
Q10279
|
O13286
|
SRW1_SCHPO
|
Suppressor of rad/wee1
|
Schizosaccharomyces
|
MDEFDGFTRPTSSNSSANRNSNNSMNRVENNNSNSDSANTVDSRGDAHTRMRQGFEKSFPSSPNKKRPRTNEGDRFIPSRDASTELWTGFTKVEGPLTPVKKKQSVADRNFTTLLRSELFGSNDETFNNSPIATPNTTIGVSTPRTDSGIDDIELTQRTPPSSSHTSSSILQNTPVTPSRKIFHYLSPRDRNKSSYGKKAQYQDNPNRTIYSLSPVRSITKDLISASRLEGRELPSIPYRVLDAPGLAGDFYLNLLDWGQCNMLAVALASRVYLWSGISSEVTVMHNFYPTDTVTSLRWVQRGTHLAVGTHNGSVEIWDAATCKKTRTMSGHTERVGALSWNDHVLSSGGRDNHILHRDVRAPEHYFRVLTAHRQEVCGLEWNSNENLLASGGNDNALMVWDKFEEKPLYSFHNHIAAVKAITWSPHQRGILASGGGTADRTIKLWNTQRGSMLHNIDTGSQVCNLLWSKQTNEFISTHGFMENEVALWNYPSVSRVGTLKGHTDRVLYLAMSPNGENIVTGAADETLRFWKLFDSKSKHSASTMSSPFDPTMKIR
|
Has a role in cell differentiation and cell cycling by negatively regulating cig2 and cdc12-associated cdc2. Down-regulates the level of cdc13, particularly in a nitrogen deprived environment. Regulator of cell cycle G1 phase progression. Prevents onset of mitosis during the pre-Start G1 period. Required for degradation of cdc13 mitotic cyclin B during G1 arrest but not during mitotic exit.
|
O13286
|
B5QW85
|
FADB_SALEP
|
3-hydroxyacyl-CoA dehydrogenase
|
Salmonella
|
MLYKGDTLYLDWLEDGIAELVFDAPGSVNKLDTATVASLGQALEVLEKQHDLKGLLLRSNKAAFIVGADITEFLSLFLVPEEQLSQWLHFANSVFNRLEDLPVPTLAAVNGYALGGGCECVLATDYRLATPDLRIGLPETKLGIMPGFGGSVRLPRMLGADSALEIIAAGKDVGAEHALKIGLVDGVVKQEKLIEGAIAVLRQAITGDLDWRAKRQPKLEPLKLSKIEAAMSFTIAKGMVAQTAGKHYPAPMTAVKTIEAAARFGREEALNLENKSFVPLAHTNEARALVGIFLNDQYVKGKAKKLTKDIETPKQAAVLGAGIMGGGIAYQSAWKGVPVIMKDINDKSLNLGMTEAAKLLNKQLERGKIDGLKLAGVISTIHPTLDYAGFDRVDAVVEAVVENPKVKKAVLAETEQKVRPETVLASNTSTIPIGELASALERPENFCGMHFFNPVHRMPLVEIIRGEKSSDETIAKVVAWASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDGADFRKVDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAAGFPQRMQKEYRDAIDALFDASRFGQKNGLGFWRYKEDSKGKPKKEEDAAVDDLLASVSQTKRDFSDDEIIARMMIPMINEVVRCLEEGIIASPAEADMALVYGLGFPPFHGGAFRWLDTQGSAKYLDMAQQYQHLGPLYEVPEGLRNKARHNEPYYPPVEPARPVGSLKTA
|
Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate.
|
B5QW85
|
B7LVL1
|
RPOZ_ESCF3
|
Transcriptase subunit omega
|
Escherichia
|
MARVTVQDAVEKIGNRFDLVLVAARRARQMQVGGKDPLVPEENDKTTVIALREIEEGLINNQILDVRERQEQQEQEAAELQAVTAIAEGRR
|
Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
|
B7LVL1
|
B0BWS1
|
MURB_RICRO
|
UDP-N-acetylmuramate dehydrogenase
|
spotted fever group
|
MLILPIVKGEYKKDYNLKHLTWFKVGGNAEIFFKPLDSEDLKSFLIQNKQKLPIKTFGAGSNIIIRDGGIEGVVIKLGQNFSNIEFIDNHLIVGSSCLNYNLAKFCQANAISGFEFLVGIPGTIGGGVAMNAGAYGSEFKDIVVQIEAIDFAGNFLTFTNEEIGFKYRSNNLPKNLIILKVIFKINKGDSENILLRMNEINNARSSTQPIKERTGGSTFANPEGCKSWELIDKAGLRGYRIGGASMSELHCNFMINNGDATAKDLEDLGNFVQQKVCEDSGVKLEWEIKRIGRHP
|
Cell wall formation.
|
B0BWS1
|
A7N9L6
|
YIDC_FRATF
|
Membrane protein YidC
|
Francisella
|
MKANHIRILLLVTIAIMFISLMGKWEQTFPADNTKQQTSATQNNSHYDNADSSTNTDVTITDAKSSLAKETNFSKYDNAKSITINTVVFKDVKVSLLDGAIISASLKDYSISLDDKTPMSLLTDKSGSEYIAKSTIVVNKQPISVNFEDQGIKIENSKQILTLTGSADGLQITRTYTFDDTKYNISVSQNIKNTTSAPVNVIVDDSFARDFDPAGDSFSLLNAHSYTFTGVAYSTAKDSFRKESFKDISKTNGQPTVINSDGQGWVAFLQHYFVSAWIPQSTNAKIYYKNLNGDVFEAGAFTGATIAPNQSENISSILYTGPIIKANLVDLAPNLEKTLDYGMLSFFSEIIFWVMNHIHSLVGNWGLAIILVTCLIKLIFYPLSAKSYRSMAKMRMLQPRIKRLQETYKDDRQALGKKMMELYKEEKVNPLSGCLPMLIQIPIFISLYWVLLESVELRQAPFIFWIHDLSMKDPYFVLPVLMGLSMFLQQKLSPAPADPMQAKVMMFLPVIFTFLFASFPSGLVLYWLTNNLISISQQWIITRHYQATHKK
|
Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins.
|
A7N9L6
|
B1JTU4
|
G6PI_BURCC
|
Phosphohexose isomerase
|
Burkholderia cepacia complex
|
MTLKSLPAWTALQSHFEQIRHARLRDWFAPENDRAPTRAERFTIPGGGLAADFSKNRIDDETLRLLVQLARDAGVEARRDAMFAGEIVNPTEGRAALHTALRATDPQAPFHAQVSAERAKMATFARAVRSGTWTGYTGKRIRHVINIGIGGSDLGPKMVVHALHHVATPEISTHFVSNVDGADLARVLEQVDPEETLAIIVSKTFTTLETMTNARSLRDWFVARGCPEDALAKHFVGVSANPAEVVKFGIAADNVFEMWDWVGGRYSLWSAVGLSIMIAIGPEQFDELLAGANDMDRHFREAPLERNLPVLLGLIGIWYRNFFGSQSYLVAPYSEALHYLPSYLQQLEMESNGKSARLDGTFVDYPTSAVTWGEPGTNGQHAFFQMLHQGPTIVPIDFIAVLTPEHPLASHHPKLLANCFAQSEALMLGRTLEEARKVAGPGKEALAPHLTFPGNRPTTTLLVDALTPRTLGALIALYEHKVLVQATVWDINPFDQWGVELGKILGKVVEADLSAESVDPAKHDSSTTALIERARAALKR
|
Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
|
B1JTU4
|
A9MQG7
|
KEFF_SALAR
|
Quinone oxidoreductase KefF
|
Salmonella
|
MILIIYAHPYPHHSHANKRMLEQAGTLENVEIRSLYHLYPDFNIDVAAEQQALSRATLIVWQHPMQWYSVPPLLKLWMDKVLAHGWAYGHGGTALHGKHLLWAVTTGGGENHFTIGSHPGFDVLSQPLQATALYCGLTWLPPFAMHCTFICDDDTLQAQARHYKQRLLAWQEANHG
|
Regulatory subunit of a potassium efflux system that confers protection against electrophiles. Required for full activity of KefC. Shows redox enzymatic activity, but this enzymatic activity is not required for activation of KefC.
|
A9MQG7
|
Q87MX4
|
RNFA_VIBPA
|
Rnf electron transport complex subunit A
|
Vibrio
|
MTEYVLLLVGTVLVNNFVLVKFLGLCPFMGVSKKLETAIGMGLATTFVLTLASVCAYLVESYILRPLGIEYLRTMSFILVIAVVVQFTEMVVHKTSPTLYRLLGIFLPLITTNCAVLGVALLNINENHNFIESIIYGFGAAVGFSLVLILFASMRERIAAADVPVPFKGASIAMITAGLMSLAFMGFTGLVK
|
Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
|
Q87MX4
|
Q8Z8G0
|
NAGB_SALTI
|
Glucosamine-6-phosphate isomerase
|
Salmonella
|
MRLIPLSTAEQVGKWAARHIVNRINAFKPTTDRPFVLGLPTGGTPLTAYKALVEMHKAGEVSFKHVVTFNMDEYVGLPKEHPESYHSFMHRNFFDHVDIPAENINLLNGNAPDIDAECRQYEEKIRSYGKIHLFMGGVGNDGHIAFNEPASSLASRTRIKTLTHDTRVANSRFFDGDVNQVPKYALTVGVGTLLDAEEVMILVLGHQKAQALQAAVEGNVNHMWTISCLQLHPKAVVVCDEPSTMELKVKTLKYFNELEAENIKGL
|
Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
|
Q8Z8G0
|
A0M591
|
RL16_GRAFK
|
50S ribosomal protein L16
|
Gramella
|
MLQPKRTKYRKQQKGRMKGLSQRGHRLSNGTFGIKSMDSSFVTARQIEAARIAATRYMKREGSIWIKIFPDKPITKKPLEVRMGKGKGAVEYWAAVVKPGRIMFEIGGVPMDVAKEALRLAAQKLPVRTKFVVARDYQE
|
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
|
A0M591
|
C1FKP7
|
FOLD_CLOBJ
|
Methenyltetrahydrofolate cyclohydrolase
|
Clostridium
|
MTKILYGNEVALKIKEDLNLRIDKLKEKNIIPKLAILRMGNKPDDIAYERSIIKSCEKLNIETKVEELNEDILEEDFLKLMESLNNEKEIHGILVFRPYPKHLNENTINSSIALNKDVDCMHPLNLERIFEGDLNQFVPCTPEAVIEILKYYDIDLKGKNIVIINRSMVVGKPLSMMVLSNNATVTICHSKTIDLPSITKKADIVVTAIGKAKLIKEEYFNEDSIVMDVSINVDENGKLCGDVDFENVKEKVGAITPVPKGVGSVTTTLLLKHIVDAAERNS
|
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
|
C1FKP7
|
Q7V3M7
|
GATB_PROMP
|
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
|
Prochlorococcus
|
MKNLEPWEAVIGLETHVQLNTKSKIFTAASTAFGDEPNTHIDPVVCGLPGTLPVLNKTVLEYAVKTSLALNLNVAEHCKFDRKQYFYPDLPKNYQISQFDEPLAENGWLEVEIAEKDKETYLKKIGIERLHMEEDAGKLVHIGSDRLAGSKYSLVDYNRAGIALVEIVSKPDIRTGREASEYASEIRRTVRYLGVSDGNMQEGSLRCDVNISVRRGPNAPFGTKVEIKNMNSFSAIQKACEYEIERQIDVYENGGEIYQETRLWDEAKQLTKSMRLKEGSSDYRYFPDPDLGPIEISKEQKDQWLDELPELPSKKRQKYVKELGLSPYDSRVISDEVFMANFFEETVANGADPKLASNWITSDIVGYLKSNKQSFAELKLSPINLAEMINMISKKVISGKIAKEILPELIQDNISPQKVVEEKGLAMISDSASISPIIEELIIEYPKEVKSFKDGKTKLLGFFVGQLMKKTKGKADPKLANKLISEKLNS
|
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
|
Q7V3M7
|
P22679
|
EFTU_METH1
|
Elongation factor Tu
|
Metamycoplasma
|
MAKLDFDRSKPHVNIGTIGHVDHGKTTLTAAIATVLAKKGLAEARDYASIDNAPEEKARGITINTSHIEYQTEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPKIVVFLNKIDMFKDDEREEMVGLVEMDVRSLLSEYGFDGDNAPIIAGSALKALQGDPEYEKGILELMDAVDTYIEEPKRETDKPFLMAVEDVFTITGRGTVATGRVERGVLQLNEEVEIVGLKPTKKTVVTGIEMFRKNLKEAQAGDNAGLLLRGIDRSEVERGQVLAKPKTIVPHTQFEATVYVLKKEEGGRHTPFFHNYKPQFYFRTTDVTGGIEFKPGREMVVPGDNVELTVTLIAPIAIEEGTKFSIREGGRTVGAGSVTKILK
|
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
|
P22679
|
P51010
|
TKT1_XANFL
|
Transketolase 1
|
Xanthobacter
|
MSSRTSDSVTSHDRLANAIRFLAIDAVEAANSGHPGLPMGAADIATVLFTKVLKYDPSRPFWPDRDRFVLSAGHGSMLLYSVLHLAGYEKVTIDEIKRFRQLGSLTPGHPENFVTEGIETTTGPLGQGIATAVGMAMAERLLAARFGSDVVDHYTYALASDGDLMEGISQEAADLAGHLKLSKLIVMWDDNKISIDGPTSISGSTNQLARFAASGWATAAVDGHDPEAILAALEAAKASDRPTLIACRTTIGFGSPKKAGSEKVHGSPLGAEEIVATRAALGWEAPAFVVPEDALNGWRAAGAAGRAAREAWEARFAARPAEERAEFERRVAGTLPAALEGAIVAVKEKAVKDGGAVATRKSSEMVLDFITPAVPEMVGGSADLTGSNNTKAKGAKSVTPDDFSGSFIHYGVREHGMAAAMNGMALHKGLIPFSGGFMVFSDYCRPAIRLAALMGERVIHVLTHDSIGLGEDGPTHQPVEHLAALRAIPNLLVMRPCDTVETAECWQIALQSTDRPSALILSRQNLPLLRTDATAVNRSAEGAYEILAASGPAQASLFATGSEVSLAVEAAKLLEAQGVPTRVVSISSFELFLERPAAERAKVIGDAPAKVAVEAAIRMGWDAIVGSNAAFVGMTSFGASAPAKELYAHFGITAQQVAARALDQLRQA
|
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.
|
P51010
|
B3PHI3
|
MDH_CELJU
|
Malate dehydrogenase
|
Cellvibrio
|
MKAPVRVTVTGAAGQISYSLLFRIAAGDMLGKDQPVILQLLEITPALKALQGVAMELDDCAFPLLAGIVTTDDPSVAFKDSDYALLVGARPRGPGMERKDLLAANAAIFSVQGKAINDHASKNIKVLVVGNPANTNALIAQRNAPDISPRQFTAMTRLDHNRALSQLATKTGTSINNITKALIWGNHSSTQYPDLHNTLVDGKPALSLVDQAWYESDYIPTVQQRGAAIIAARGASSAASAANAAINHIRDWALGTPANDWVSMGVYSDGSYGIEKGLIYSFPCVCKNGDWEIVQGLDINEFSRAKMTATEKELQEERDAVKELLPA
|
Catalyzes the reversible oxidation of malate to oxaloacetate.
|
B3PHI3
|
P81596
|
TO1C_HADVE
|
Omega-atracotoxin-Hv1c
|
Hadronyche
|
SSTCIPSGQPCPYNENCCSQSCTFKENENGNTVKRCD
|
Inhibits insect, but not mammalian, voltage-gated calcium channels (Cav).
|
P81596
|
Q03IN1
|
DAPEL_STRTD
|
N-acetyldiaminopimelate deacetylase
|
Streptococcus
|
MTLDLIKIRRDLHQIPEIGLEEFKTQAYLLERIAEMTEGKDFVEQRTWRTGILVFLHGSAPEKTIGWRTDIDGLPIVEETGLDFKSIHEGRMHACGHDIHMTTALGLLDQMLQVQPKNNMLFLFQPAEENEAGGMLMYEDGAFGDWLPDEFYGLHVRPDFKVGDIATNTNTLFAGTCEVLVTFKGKGGHAAFPHEANDALVAASYFITQVQTIVSRNVDPIQGGVVTFGSFHAGTTNNVIAETAEVYGTIRTLTQEMSLLIQKRVRQIAEGVAASFGMEVDIMLKQGGYLPVENNPALAKELMAFFDASPMVNLIDCLPAMTGEDFGYLLSKVPGVMFWLGIDTPYALHHPKMSPNEEALAFAVSEIGKFLKYKAED
|
Catalyzes the conversion of N-acetyl-diaminopimelate to diaminopimelate and acetate.
|
Q03IN1
|
Q9SUH5
|
AUG8_ARATH
|
ROP1 enhancer 2
|
Arabidopsis
|
MDVATDTTRRRLLPSDKNNAVVATRRPRTMEVSSRYRSPTPTKNGRCPSPSVTRPTVSSSSQSVAAKRAVSAERKRPSTPPSPTSPSTPIRDLSIDLPASSRRLSTGRLPESLWPSTMRSLSVSFQSDSVSVPVSKKERPVSSSSGDRTLRPSSNIAQKHKAETTSVSRKPTPERKRSPLKGKNNVSDLSENSKPVDGPHSRLIEQHRWPSRIGGKITSNSLNRSLDLGDKASRGIPTSGPGMGPSLRRMSLPLSSSSRPLHKTSSNTSSYGGLVSPTKSEDNNIARTSGAQRLLSAGSLDRATLATAVARLHPLPAPGSRPASPSRTSFLSSSSISRGMSTSRGVSPSRGLSPSRGLSPTRGLSPSRGLSPSRGTNTSCFARPSTPPSRGISPSRIRQTTTSTQSSTTTSVLSFITDVKKGKKASYIEDVHQLRLLHNRYLQWRFAIARAESVMYIQRLTSEETLFNVWHAISELQDHVTRQRIGLQQLKLEIKLNSLLNDQMVSLEDWATLERDHVSSLVGAISDLEANTLRLPATGGTKADTESLKAAMSSALDVMQAMGSSIWSLLSKVEEMNIMVTELAVVVTKESSMQGKCEDLLASTAIMQIEECSLRTHLIQTRREEGEDAETPPPLLPLSKFPWP
|
Contributes to the assembly of the acentrosomal spindle and phragmoplast microtubule arrays as part of the augmin complex.
|
Q9SUH5
|
A0A0U1LSP0
|
CCTP_TALIS
|
Cyclochlorotine biosynthesis protein P
|
Talaromyces sect. Islandici
|
MASQSAHLVKTHQLWELLRHRTKTGSYELDGDSLHIADVVATAQQTSTPRLSEDPKVIKGLQDSVDVLFDHLAKGWYVYGVNTGFGGSADSRTTEVIELQKALMQLTQTGILTTPSDGSAIPGHSTPFEWVRAAMVVRCNASLRGHSAVSLPIIKAIINLLVHGLTPVVPLRGTVSASGDLMPLAYVTGSIEGNPDTLLEKNGKVLPSPKALQEAGLAPVFLGPKEGLGLINGTASSAGLGALVVAQAHSLAFLTQVLTGGAVEALRGSSESFHPFIARARPHPGQIECARNIAYFLRGSHLSRDVLAPKDRRREDLAQDRYSLRSAPQWIGPQLEDLLLADQQISIELNSSCDNPLVDSETNDIYYGCNFQAAAVTSAMEKVRLAMQMFGRMLFAQSTEMIDVHLSGGLPANLAADNPSISFTMKGVDINMAAYMAELSYLANPMSSHVQAAEMHNQSVNSMAFASARISHDAIDVLTKMCACSVFTVCQALDLRALHMAFIADATKALASTIELKFSAKVEAGQLNSLQMLIQAHVTRAWGLTGKLDLHARCESLIDSALPIVLCHVAGDVADIIEWKTQAIEVVWNVWTNTFASFSAAPHTSQLLGAGSRLLYNFVRKTLGVPFHEGFVEHPTADSQTLHSRPKKTIDILANLSDSSNSKRDIERERLKGEKPTRSILITMEGKTSRYQDEAHDSAGSFNEETEGLMSGLHRSTKKRKLSSIVKLATPFLIVSFILNIVQLAYITVRRPECYSLYAKLKEHEITVPFRYATEYSDDEHTHEEKDALWNAIDISEGFVAISNDESDRLGLPRSKTFPWDANKGIYVSHGHHALHCTVLLHAYTYDAHQGKKPLVSYHHIEHCLDLLRQDIMCYANDVMDYTPDHGDNFLTGEGQQRKCRDWNKLSAWVKERSACYKTINITRAGEDHGVAHQLDRYTYCPPGSPYEPLIKAFKDLGRVNTGNLAADGFHELTPEELAAEAQAVAEHNKQILADEG
|
Phenylalanine aminomutase; part of the gene cluster that mediates the biosynthesis of the mycotoxin cyclochlorotine, a hepatotoxic and carcinogenic cyclic chlorinated pentapeptide . Cyclochlorotine is formed by the nonproteinogenic amino acids L-2-aminobutyrate (2Abu), L-beta-phenylalanine (beta-Phe), the unique L-cis-3,4-dichloroproline Pro(Cl(2)) and two L-serines (Ser) . The condensation of the 5 building blocks is performed by the cyclochlorotine synthetase cctN, a nonribosomal peptide synthetase . The assembled linear pentapeptide is then assumed to be released through cyclization by the terminal condensation-like domain of cctN . Incorporation of the alternative substrates allo-threonine or alanine by the domains A3 or A1 respectively may lead to the production of the variants hydroxy-cyclochlorotine and deoxy-cyclochlorotine, respectively . CctP probably acts as a phenylalanine aminomutase and provides the uncommon building block beta-Phe . Furthermore, 2Abu can be synthesized from threonine by one of the threonine dehydratases and transaminases localized outside of the cluster . The biosynthesis of the unusual dichloroproline moiety remains elusive since the actual halogenase still awaits to be detected, with the possibility that proline halogenation is accomplished by a so far unknown type of halogenase . Finally, the cluster encoded transporters cctQ and cctS are most likely responsible for cyclochlorotine secretion and thereby may contribute to intrinsic resistance . The functions of the remaining proteins encoded by the cluster (cctM, cctO, cctR and cctG) have not been identified yet .
|
A0A0U1LSP0
|
P31273
|
HXC8_HUMAN
|
Homeobox protein Hox-3A
|
Homo
|
MSSYFVNPLFSKYKAGESLEPAYYDCRFPQSVGRSHALVYGPGGSAPGFQHASHHVQDFFHHGTSGISNSGYQQNPCSLSCHGDASKFYGYEALPRQSLYGAQQEASVVQYPDCKSSANTNSSEGQGHLNQNSSPSLMFPWMRPHAPGRRSGRQTYSRYQTLELEKEFLFNPYLTRKRRIEVSHALGLTERQVKIWFQNRRMKWKKENNKDKLPGARDEEKVEEEGNEEEEKEEEEKEENKD
|
Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
|
P31273
|
P17219
|
PTTH_BOMMO
|
Prothoracicotropic hormone
|
Bombyx
|
MITRPIILVILCYAILMIVQSFVPKAVALKRKPDVGGFMVEDQRTHKSHNYMMKRARNDVLGDKENVRPNPYYTEPFDPDTSPEELSALIVDYANMIRNDVILLDNSVETRTRKRGNIQVENQAIPDPPCTCKYKKEIEDLGENSVPRFIETRNCNKTQQPTCRPPYICKESLYSITILKRRETKSQESLEIPNELKYRWVAESHPVSVACLCTRDYQLRYNNN
|
Peptides P2K and P6K are presumed to be cleaved post-translationally and may play some unknown physiologically or developmentally important functions.
|
P17219
|
Q9M2S4
|
LRKS4_ARATH
|
L-type lectin-domain containing receptor kinase S.4
|
Arabidopsis
|
MSQTFAVILLLLIFLTHLVSSLIQDFSFIGFKKASPNLTLNGVAEIAPTGAIRLTTETQRVIGHAFYSLPIRFKPIGVNRALSFSTSFAIAMVPEFVTLGGHGLAFAITPTPDLRGSLPSQYLGLLNSSRVNFSSHFFAVEFDTVRDLEFEDINDNHVGIDINSMESSISTPAGYFLANSTKKELFLDGGRVIQAWIDYDSNKKRLDVKLSPFSEKPKLSLLSYDVDLSSVLGDEMYVGFSASTGLLASSHYILGWNFNMSGEAFSLSLPSLPRIPSSIKKRKKKRQSLILGVSLLCSLLIFAVLVAASLFVVRKVKDEDRVEEWELDFGPHRFSYRELKKATNGFGDKELLGSGGFGKVYKGKLPGSDEFVAVKRISHESRQGVREFMSEVSSIGHLRHRNLVQLLGWCRRRDDLLLVYDFMPNGSLDMYLFDENPEVILTWKQRFKIIKGVASGLLYLHEGWEQTVIHRDIKAANVLLDSEMNGRVGDFGLAKLYEHGSDPGATRVVGTFGYLAPELTKSGKLTTSTDVYAFGAVLLEVACGRRPIETSALPEELVMVDWVWSRWQSGDIRDVVDRRLNGEFDEEEVVMVIKLGLLCSNNSPEVRPTMRQVVMYLEKQFPSPEVVPAPDFLDANDSMCLDERSGSAGEFEDFVDSARFYSGPNETTTSSIFSFSGKTRTDPR
|
Involved in resistance response to the pathogenic oomycetes Phytophthora infestans and Phytophthora capsici and to the pathogenic bacteria Pseudomonas syringae.
|
Q9M2S4
|
Q0VTD8
|
TSAC_ALCBS
|
tRNA threonylcarbamoyladenosine biosynthesis protein TsaC
|
Alcanivorax
|
MNQHLLSAAQIIQEGGVVAYPTESVYGLGCDPFNRNAVMQLLAIKHRPVSKGLILIGESLAQLAPYLHLNEQQSAQLEKKWPAPITYLVDASDRLPAWVRGEHRKVAVRVPDHPLARQLCQLAGQPIISTSANISGRPAARNRYQVARQLGNQLDFIVSGACDRAAKPSTIIDLESGRILRP
|
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.
|
Q0VTD8
|
Q9KA09
|
Y2485_HALH5
|
UPF0122 protein BH2485
|
Halalkalibacterium (ex Joshi et al. 2022)
|
MLDKTLRMNYLFDFYQSLLTEKQRKYMSLYYLDDFSLGEIAEEFDVSRQAVYDNIKRTEAMLEEYEEKLSLLAKFEKRSEILQQLKEAVDKQATSEELMALLESLDTLE
|
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.
|
Q9KA09
|
B9KK25
|
BCHB_CERSK
|
Light-independent protochlorophyllide reductase subunit B
|
Cereibacter
|
MKLTLWTYEGPPHVGAMRVATGMTGMHYVLHAPQGDTYADLLFTMIERRGKRPPVSYTTFQARDLGSDTAELFQSACRDAYERFQPQAIMVGSSCTAELIQDDTGGLADALSLPVPVVHLELPSYQRKENFGADESFLQICRKLARPMERTEKVSCNLLGPTALGFRHRDDILEVTRLLEGMGIAVNAVAPMGASPADIARLGAAHFNVLLYPETGESAARWAEKTLKQPYTKTVPIGVGATRDFVAEVAALAGVAPVADDSRLRQPWWSASVDSTYLTGKRVFLFGDATHVIAAARVARDEMGFEVVGMGCYNREFARPMRAAAKGYGLEALVTDDYLEVEEAIQALAPELILGTQMERHIAKRLGIPCAVISAPVHVQDFPARYSPQMGFEGANVLFDTWIHPLTMGLEEHLLTMFREDFEFHDEAGPSHHGGKAVPASAPRADEAAEALPATGAETAEGGSIPPEAVPPAAAAAAEAPAGEIVWLTDAERELKKIPFFVRGKARRNTEKFAAEKGLTRISIETLYEAKAHYAR
|
Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (BchN-BchB) is the catalytic component of the complex.
|
B9KK25
|
Q6MZT1
|
R7BP_HUMAN
|
R7 family-binding protein
|
Homo
|
MSSAPNGRKKRPSRSTRSSIFQISKPPLQSGDWERRGSGSESAHKTQRALDDCKMLVQEFNTQVALYRELVISIGDVSVSCPSLRAEMHKTRTKGCEMARQAHQKLAAISGPEDGEIHPEICRLYIQLQCCLEMYTTEMLKSICLLGSLQFHRKGKEPGGGTKSLDCKIEESAETPALEDSSSSPVDSQQHSWQVSTDIENTERDMREMKNLLSKLRETMPLPLKNQDDSSLLNLTPYPLVRRRKRRFFGLCCLISS
|
Regulator of G protein-coupled receptor (GPCR) signaling. Regulatory subunit of the R7-Gbeta5 complexes that acts by controlling the subcellular location of the R7-Gbeta5 complexes. When palmitoylated, it targets the R7-Gbeta5 complexes to the plasma membrane, leading to inhibit G protein alpha subunits. When it is unpalmitoylated, the R7-Gbeta5 complexes undergo a nuclear/cytoplasmic shuttling. May also act by controlling the proteolytic stability of R7 proteins, probably by protecting them from degradation.
|
Q6MZT1
|
A3CNT5
|
HIS1_STRSV
|
ATP phosphoribosyltransferase
|
Streptococcus
|
MSQITIALTKGRIEKDTVKLLTQAGFDMSFMADKGRSLIFESPDSRFRFLLVKGPDVTTYVRHGVADLGIVGKDILFEHPTGYLELLDLNFGLCKFSLASVPSYDPHDHKRKRIATKYPTVATDYFNQKGEDVEIISIQGSVEISPVLGLADAIVDIVETGHTLSANGLLVFEDICRVSARLIANQASLKNNPDIMPFVAKIESLVGRREVAFK
|
Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
|
A3CNT5
|
Q9KGF8
|
ISPD_HALH5
|
MEP cytidylyltransferase
|
Halalkalibacterium (ex Joshi et al. 2022)
|
MEYSVVIPAAGQGKRMRAGHNKQFIELGGKPILAHTLAVFEQDDWCTNVVIVANEQEIEEMGELANRYQISKAKKIVAGGRERQESVFAGLKALSQDGLVLIHDGARPFVTEKEIHSLVETAAKTHAAVLAVPVKDTIKRVEGEAVLETMPREELWAVQTPQAFDLALIKQAHQKAENEQMLGTDDASLMEWLGYSVAVVQGSYFNFKLTTPEDLLFAEAILAEKERR
|
Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
|
Q9KGF8
|
P36250
|
RL11_LIBAS
|
50S ribosomal protein L11
|
Liberibacter
|
MAKVVSRIVKLQIESGSAKPSPPVGPAIGQAGIPIMAFCKAFNAATEGMEKGIPIPTTVTCYKDKSFTFTMSQPPVSFFLKKEVGIKSGSKLPGKESCGSITRENIRKIAQLKMQDMGAIDIEGAMRMVEGSACSMGISVVD
|
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
|
P36250
|
Q5GAM8
|
RNS12_MOUSE
|
Probable inactive ribonuclease-like protein 12
|
Mus
|
MVLMVVVFLLLLFWENELTEDVVLTSIEQLHVDYPQNAVPLRYCNYMILQRVIREPDHRCRKVHVFIHERPQKINRVCTSSKKMSCPNDSDLFCFQSETKFRMTVCQLIDGTTYPACRYQISPIKGFVLVTCDDLGPVDLQGYVE
|
Does not exhibit any ribonuclease activity.
|
Q5GAM8
|
P07552
|
QCR10_BOVIN
|
Ubiquinol-cytochrome c reductase complex 6.4 kDa protein
|
Bos
|
MLTRFLGPRYRQLARNWVPTASLWGAVGAVGLVWATDWRLILDWVPYINGKFKKDD
|
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. QCR10 has a role in CIII assembly and RIP1 stability.
|
P07552
|
A9HS61
|
TRMD_GLUDA
|
tRNA [GM37] methyltransferase
|
Gluconacetobacter
|
MTWRATVLTLFPDMFPGPLGQSLAGRALEGGLWSVEARNLREYGLGRHRVVDDTPFGGGAGMVMRPDVVSAAIRDVAPAGRPLVYPTPRGRPLRQDDVRRYAGGPGLVVLCGRYEGVDERALEACGAEQVSIGDYVLSGGEMAALVLLDSCVRLIPGVMGSDASGTEESFSDGLLEYPHYTKPASWEGRDVPDILLSGHHAAIAGWRQTESETATRTRRPDLWAAHLERTGCTDRQF
|
Specifically methylates guanosine-37 in various tRNAs.
|
A9HS61
|
Q84WD3
|
DRL26_ARATH
|
Probable disease resistance protein At4g19060
|
Arabidopsis
|
MDIAKKFISEIDDKLESKSEFDKELEKIKSSFNEEYEKWSSGKQRGSSSKHGNQSTHGDSSPTRNSSGSSKKGRPKANRVETSSELPDHLIRGFINEKLFLKNFLLKQKESEEFKTLAIVGKYGVGKTTLCQAVFNDEDVKQVYFPRIWVSMYSKETKEDEDPKIDVVKRILRSLGVEDEMFKHIKTEAEEEKSIKDEAGEREEETVKEKELARLLYALHLNLIGKKYLIVLDDVWEDNEWDQRLDDEKKQQEKSHLSCGFPKGFGGKVIMTSRDERLAKAIVGEEENLQRLFPRSDAESLWEIYIDAVPTKVDDAAATNLGDAVATNAGDAVAPKVNPRYPGRYKQELMDKSCGIPLAARMLAKIEPVKVDEIGNIDRKQSF
|
Possible disease resistance protein.
|
Q84WD3
|
Q0I4R8
|
TGT_HAES1
|
tRNA-guanine transglycosylase
|
Histophilus
|
MKFTLHKTNGMARRGTMTFNRPQGEFTVETPAFMPVGTYGTVKGMTPEEVRVTGAEILLGNTFHLWLRPGQEIMRQHGDLHDFMQWHRPILTDSGGFQVFSLGKLRKITEEGVKFQNPINGERIFLSPEKSMEIQYDLGSDIVMIFDECTPYPATFDYAKKSMEMSLRWAKRSRERFDELGNKNALFGIVQGSTFEDLRKLSIEGLINIGFDGYAVGGLAVGEPKEDMHRILAYVCPQLPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVSNGIVKIRNAKYRNDTTSLDPECDCYTCKHYTKAYLYHLDKCGEILGARLNTIHNLHYYQRLMAQIRQAIEEDRFEDFVVEFYKKIGKSVPTR
|
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
|
Q0I4R8
|
Q1IWG2
|
HEM1_DEIGD
|
Glutamyl-tRNA reductase
|
Deinococcus
|
MPPLAPLDFAVIGLNHQTAPVEVREQAAVRAGDEGKVLQHLSRYAREVMLLNTCNRTEVYLAGLQGDPLRAFESGWGRALDGHLYVHRGEAAATHLYRVAAGLDSLVIGETQIQGQVKRAWQEAHARGLSGTLLNKVAQGALAAGKRVRSETGLSDKVVSVSSAAVELAEAALGELRHRTALILGAGETAELTLTHLRAAGVQDVIVVNRTEARARQLADKLGGRACAAEYLHEVLPEADVVIASSAAPHYVLHGEGVRAALAKRPERPIFLIDISVPRILDPDIRAVSGAHLYNLDDLTAIVSRNLQSRRAALPYAEAIIREAVADLLRWHLTREAQLGRRAVALASD
|
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
|
Q1IWG2
|
P66029
|
RHO_MYCBO
|
ATP-dependent helicase Rho
|
Mycobacterium tuberculosis complex
|
MTDTDLITAGESTDGKPSDAAATDPPDLNADEPAGSLATMVLPELRALANRAGVKGTSGMRKNELIAAIEEIRRQANGAPAVDRSAQEHDKGDRPPSSEAPATQGEQTPTEQIDSQSQQVRPERRSATREAGPSGSGERAGTAADDTDNRQGGQQDAKTEERGTDAGGDQGGDQQASGGQQARGDEDGEARQGRRGRRFRDRRRRGERSGDGAEAELREDDVVQPVAGILDVLDNYAFVRTSGYLPGPHDVYVSMNMVRKNGMRRGDAVTGAVRVPKEGEQPNQRQKFNPLVRLDSINGGSVEDAKKRPEFGKLTPLYPNQRLRLETSTERLTTRVIDLIMPIGKGQRALIVSPPKAGKTTILQDIANAITRNNPECHLMVVLVDERPEEVTDMQRSVKGEVIASTFDRPPSDHTSVAELAIERAKRLVEQGKDVVVLLDSITRLGRAYNNASPASGRILSGGVDSTALYPPKRFLGAARNIEEGGSLTIIATAMVETGSTGDTVIFEEFKGTGNAELKLDRKIAERRVFPAVDVNPSGTRKDELLLSPDEFAIVHKLRRVLSGLDSHQAIDLLMSQLRKTKNNYEFLVQVSKTTPGSMDSD
|
Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template.
|
P66029
|
A3PII0
|
SELO_CERS1
|
Protein adenylyltransferase SelO
|
Cereibacter
|
MTFRFDNSYARDLEGFYVDWPAAPVPAPRLLRLNRPLAEELGLDPDLLEREGAEIFSGRRLPEGAHPLAQAYAGHQFGGFSPQLGDGRALLIGEITDRAGRRRDLQLKGSGRTPFSRGADGKAALGPVLREYLVGEAMHGLGIPTTRALAAVATGEPLLRQEGERPGAILTRVAASHIRVGTFQFFAARSDIERVRRLADYAIARHYPELASAPEPYLAFYEAVAEAQAQLVARWMLVGFIHGVMNTDNMTISGETIDYGPCAFMEGYDPGTVFSSIDLQGRYAYGNQPFILAWNLARLGEALLPLLDADAERAADKANSVLETVGARYQGHWLAGMRAKLGLSGAEEGDARLAEDLLEAMRSQRADWTLTFRRLADAVTDEGALRPLFRDGSALEAWLPRWRDRLAPDAAQRMRATNPIYIARNHRVEEALAAAHAGDLAPFDRLLEALAEPFTERADRELFALPAPEGFDDSYRTFCGT
|
Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
|
A3PII0
|
C0MBZ4
|
RLMN_STRE4
|
tRNA m2A37 methyltransferase
|
Streptococcus
|
MKPSIYGLTRDELIAWAIDNGQKAFRATQIWDWLYRKRVQSFDEMTNISKEFVAILKDSFCINPLKQRVAQESADGTVKYLFELPDGMLIETVLMRQHYGQSVCVTTQVGCNIGCTFCASGLIKKQRDLNSGEITAQIMMVQNYFDKRAQDERVSHVVVMGIGEPFDNYQNVMTFLRTINDDHGLAIGARHITVSTSGLAHKIREFANEGVQVNLAVSLHAPNNELRSSIMRINRSFPLDKLFSAIEYYIETTNRRVTFEYIMLNKVNDGVEQAQELADLTKRIRKLSYVNLIPYNPVSEHDQYSRSPKERVAAFYDILKKNGVNCVVRQEHGTDIDAACGQLRSNTMKKDRQKAAAART
|
Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs.
|
C0MBZ4
|
Q9SW07
|
GDU2_ARATH
|
Protein GLUTAMINE DUMPER 2
|
Arabidopsis
|
MQTMEGRQYNYQDSINASSSMVVPHSPWHSPVPYLFGGLAAMLALICVALLILACSYWRLSGSAERDLEAGDDAKPDNDTNKTKHTEMPEKFLVIMAGDVRPTYLATPATRSEQSCTCGDHNEEEGRRG
|
Probable subunit of an amino acid transporter involved in the regulation of the amino acid metabolism. Stimulates amino acid export by activating nonselective amino acid facilitators.
|
Q9SW07
|
A0R528
|
KSTR_MYCS2
|
HTH-type transcriptional repressor KstR
|
Mycolicibacterium
|
MTNVAVLSESELGSEAQRERRKRILDATLAIASKGGYEAVQMRAVAERADVAVGTLYRYFPSKVHLLVSALGREFERIDAKTDRAALAGGTPYQRLNFMVGKLNRAMQRNPLLTEAMTRAFVFADASAAGEVDHVGKLMDSMFARAMSDGEPTEDQYHIARVISDVWLSNLLAWLTRRASATDVSKRLDLAVRLLIGTEEQPKI
|
Controls the expression of genes used for utilizing diverse lipids as energy sources.
|
A0R528
|
A9W6Q3
|
NADD_METEP
|
Nicotinate mononucleotide adenylyltransferase
|
Methylorubrum
|
MRIGLYGGSFNPAHAGHLHVSRTALRRLRLDRVWWLVTPGNPLKDHGVLAPLDERVAQARALATDPRIAVTGFEGGIGSRYTADTLRWLVRRQPALHFVWIMGADSLGTFHRWRRFDEILSLMPVAVIDRPGYTLTAPSARAAQAFASARIQEADAPTLAIRPTPAWTFLHGPRSALSSTALRTR
|
Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
|
A9W6Q3
|
Q5HZG9
|
ZN488_MOUSE
|
Zinc finger protein 488
|
Mus
|
MAAGTSTLLSLSGPADHMAEGKGAPLRPSVEKRWKLMEPKQTQAGMFKKMSLVDSDTAAGKGSQDEAYTELSLPTAPNKPRLDRPRACKAYTEQRHNTFTELSCLQERPGDIQAQTRKLENPEGQLGPQQLPSSFLRASGDGTVCSAWPGAPRSEQKSAFSKPAKRPAEKPKRSPMLLAGGSAEGSWELSGLITTVDIPYWAHLSTFKFMGDFWKLHTLSQNILLCNAFQGAPTPWLEHTQVQAPTSSAPSSTASRALLPPTLSSLGLSTQNWCAKCNLAFRLTADLVFHMRSHHKREHVGPDPHSKKRREEVLTCPVCHEYFRERHHLSRHMASHS
|
Transcriptional repressor . Plays a role in oligodendrocyte differentiation, together with OLIG2 . Mediates Notch signaling-activated formation of oligodendrocyte precursors . Promotes differentiation of adult neural stem progenitor cells (NSPCs) into mature oligodendrocytes and contributes to remyelination following nerve injury .
|
Q5HZG9
|
B1Y0U3
|
EFP_LEPCP
|
Elongation factor P
|
Leptothrix
|
MKIAQEIRAGNVIMHGKDPMVVLKTEYSRGGRNSATVRMKLKSLLSNSGTEVVFKADDKMDQIILDKKECTYSYFADPMYAFMDADFNQFEVEAENMGDAISYLEDGMAVEVVFYDGKAISVELPTSLVREVTWTEPAVKGDTSGKVLKPAKLATGFDIQVPIFVAQGDKIEIDTRTHEYRKRV
|
Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
|
B1Y0U3
|
Q2IPI8
|
KUP_ANADE
|
Probable potassium transport system protein kup
|
Anaeromyxobacter
|
MSQIPSPNDPPPAGAVPTSGAPAGPSATPAPSPTAGFSLPEHRPAPTGKALAALAVGALGVVYGDIGTSPLYSLKECFGGPHGVHPTDANVLGVLSLVFWAMTFVVTFKYMSFVMRADNRGEGGILALMALVGKTETTRLGRRVLLMLGLFGAALLYGDGIITPAISVLGAVEGVAVAAPAMERVVVPATVVILVFLFLFQKQGTAKVGAVFGPIMLVWFATIAVLGVRGILHDPSILRALLPTHALSFFARNGWHGFLVLGGVVLVITGGEALYADMGHFGKRPIRVAWLGLAMPALLLNYLGQGALLLHDPGAARNPFYLLAPEWALYPTIAIATAAAIVASQALISGAYSLTQQAIQLGYSPRVTIRHTSQREIGQIYLPEVNWMLGTACVALVLGFQTSSRLASAYGIAVTGTMIVTTLLFHRVMRDRWGWARWKAWPLTVLFLTVDASFFLANVVKFRDGGWFPIAAAALVFTLMSTWKRGRDALALMLKDAGLPLDLFMADVARRKVQRVAGTAVFMTSNPGGVPPVLLHHLKHNKVLHERVILVSILAHEIPFVAEAERVNARELGSGFFQVIAHYGFMETPDVPALLDSLPRRALAGPRLTIVPMETTYFLGRETLLANGPSTIPTWRKRLFIVMARNAQTASAFFGLPPNRVVEMGAQIQL
|
Transport of potassium into the cell.
|
Q2IPI8
|
O60181
|
RIB3_SCHPO
|
3,4-dihydroxy-2-butanone 4-phosphate synthase
|
Schizosaccharomyces
|
MLASIEEAVNDFRDGKFLIVLDDETRENEGDLIIAGCKVTTEQMAFLVRHSSGYVCVPMTGERLDSLEIPMMVDNNEDRMRTAYAVTLDYANGTTTGISAHDRALTTRQLANPEVTSPREFNRPGHIVPLRARDGGVLERDGHTEAAVDLCKLAGLPPVGAICELVREEDGLMSRFDDCISFGKKWGIKVITIESLKSYIKGRM
|
Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
|
O60181
|
Q9CEU0
|
AROA_LACLA
|
5-enolpyruvylshikimate-3-phosphate synthase
|
Lactococcus
|
MKLKINSQGLKGRLKVPGDKSISHRSIMFGSIAKGKTVIYDILRGEDVLSTIEAFRAMGVEIEDKGEVITVHGKGISELKAPEKALDMGNSGTSTRLLSGILAGLPFETTLFGDDSLSKRPMDRVATPLQLMGAEITGQTDKVKLPMTIKGSTHLKAIDYVLPVASAQVKSAVIFAALQAEGLTKVVEKEKTRSHTEEMLVQFGGELKVSDKTILVPGGQKLVGQKVVVPGDISSAAFWLVAALVVENSELILENVGVNETRTGIIEVIQAMGGQLEILEQDNVAKAATLKVKASQLKGTEISGDLIPRLIDELPIIALLATQAQGQTIIRDAAELKVKETDRIAVVANALNSMGAKIQPTDDGMIIQGGTKLHAPENSINTLGDHRIGMMAAIAALLVKNGEIELERAEAIQTSYPSFFDDLEQLSENI
|
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.
|
Q9CEU0
|
D1A2S9
|
PSB1_THECD
|
Proteasome core protein PrcB 1
|
Thermomonospora
|
MASHDSYTGRLPGAFMNPGTSSFTEFLASYNPDLLPGRHMTALAGGMPGNVEAPHATTIVAVTFPGGVVMAGDRRATAGNMIAQRDVEKVFRADEFSAVAIAGTAGIGMEIVRLFQVEIEHYEKMEGRTLSLEGKANRLATMIRANLGMAMQGLVAVPLFAGYDTEREVGRIFSYDPAGGRYEEHEHHSIGSGSVFARGALKKLWRPDLSAQDAALVCVQALYDAADDDSATGGPDLIRKIYPVVATVTADGFRRLPEEEVGELARIVVDGRHDSPGGPTAPLR
|
Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
|
D1A2S9
|
Q87VV6
|
PROA_PSESM
|
Glutamyl-gamma-semialdehyde dehydrogenase
|
Pseudomonas
|
MTESVLDYMTRLGRAAREASRVIGRASTAQKNRALQATAAALDEARDELSAANALDLAYGQANGLEPAMLERLALTPARIDSMIVGLRQVASLADPVGAIRDMSYRPSGIQVGKMRVPLGVVGIIYESRPNVTIDAASLCLKSGNATILRGGSEAIHSNRAIAACIARGLAEAGLPAAVVQVVETTDRAAVGALITMPEYVDVIVPRGGKGLIERVSRDARVPVIKHLDGICHVYVSAHADLPKAQKIAFNAKTYRYGICGAMETLLVDQTIAADFLPAMAAQFREKGVELRGCERTRELIDVMPATEDDWHTEYLAAILSIRVVSGLDEAIEHINHYGSHHSDAIVSDHQSQIRRFMAEVDSSSVMVNAPTSFADGFEYGLGAEIGISTDKLHARGPVGLEGLTCEKYIVIGDGQLRGHA
|
Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
|
Q87VV6
|
Q1DN93
|
ATG1_COCIM
|
Autophagy-related protein 1
|
Coccidioides
|
MAALQSPKTSSRRSKGDGDGDTRDVILGKYTKIEEIGRGSFATVYQGIHNKYRSCVAIKAVNISSLNPKLKDNLKLEIEILKGLQHPHIVALIDCDESTSCIHLVMEYCALGDLSLFIRKRDTLSKHELTRDMIAKYPNPPAGGLNEVIVRHFLKQLASALQFLRTKDLIHRDLKPQNLLLNPPPSTYAKGLLRIVPYKTREDSFTPLVGVESLPMLKIADFGFARSLPATSLAETLCGSPLYMAPEILRYEKYDAKADLWSVGTVLFEMVVGKSPFRAGNHVDLLRKIEQGEDNIRFPIQTEASPPLKKLIRSLLKRNPVERLSFKDFFESSVVKGNIPGLVDEDLQAQRERDSRLAAHAARRDSLPSRTSDGKLEDRPPSSASSPRPPPSNFTRPATSPAVRHVGSRENPDLQRVAVKARKASVASVTGSPSKEELRDHNAKGPVTEQPGPTSPAKERATTRKNSSDQRIDDILDSERERAAQDVAFERDYVVVEKRAVEVNAFADELAASPRFQQQQQQQLIPKQAGAIVRRATTTATPQLSSSPRDAMSRAVATAYNRPRTGSTHNRHNSYDRRYGPSPTSATSAISKALNKASGRLFGVSFSPPLALTKAGRSPPIGYNAFPAYPLAEGNLAVVGDGAKIQPPLDEDTKVLHIIEEIATRSDVVYGFAEVKYKQLAPLTPSMQADTAIKPVVSPEVVDTPEANDTGLTVDAIFTLSEEALVLYVKALSLLAKSMDIAGAWWARKNRGETIGNSPNVNVGCRVNNVVQWVRNRFNEVLQKAEYSRLKLLDAQRQLPYDHAHHASQVGRVSVGALAHSSDQVVISSGITAEKLMYDRALEMSRTAAINELTGEDLPGCEIAYMTAIRMLEAVLDSDEDHQLSGERAGEAANTVSNEENGEVNGLQGEDREIVAKLVASIRIRLTALKKKIALMTKRTSAPAMVSPARTPACQPPAASPVVPQASSR
|
Serine/threonine protein kinase involved in the cytoplasm to vacuole transport (Cvt) and found to be essential in autophagy, where it is required for the formation of autophagosomes. Involved in the clearance of protein aggregates which cannot be efficiently cleared by the proteasome. 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. Also involved in endoplasmic reticulum-specific autophagic process, in selective removal of ER-associated degradation (ERAD) substrates. Plays a key role in ATG9 and ATG23 cycling through the pre-autophagosomal structure and is necessary to promote ATG18 binding to ATG9 through phosphorylation of ATG9. Catalyzes phosphorylation of ATG4, decreasing the interaction between ATG4 and ATG8 and impairing deconjugation of PE-conjugated forms of ATG8.
|
Q1DN93
|
C0MGM0
|
IF3_STRS7
|
Translation initiation factor IF-3
|
Streptococcus
|
MKIIAKKDLFINDEIRVREVRLVGLEGEQLGIKPLSEAQSLADAANVDLVLIQPQAVPPVAKLMDYGKFKFEYQKKQKEQRKKQSVVTVKEVRLSPVIDKGDFETKLRNGRKFLEKGNKVKVSIRFKGRMITHKEIGAKVLADFAEATQDIAIIEQRAKMDGRQMFMQLAPISDKK
|
IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins.
|
C0MGM0
|
Q7YJY2
|
ATPI_CALFG
|
F-ATPase subunit IV
|
Calycanthus
|
MNVLPCSINTLKGLYDISEVEVGQHFYWQIGGFQVHAQVLITSWVVIAILLGSAAIAVRNPQTIPTDGQNFFEYVLEFIRDLTKTQIGEEYGPWVPFIGTMFLFIFVSNWSGALLPRKIIQLPHGELAAPTNDINTTVALALLTSVAYFYAGLTKKGLGYFGKYIQPTPILLPINILEDFTKPLSLSFRLFGNILADELVVVVLVSLVPLVVPIPVMFLGLFTSGIQALIFATLAAAYIGESMEGHH
|
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
|
Q7YJY2
|
Q5JLS2
|
CIPKC_ORYSJ
|
OsPK7
|
Oryza sativa
|
MLMATVSPARREPTPQAVRASPMPSAAAALVRRGGGGSGGTVLGKYELGRVLGQGSFAKVYQARHLETDECVAIKVLDKEKAVKGGMVHLVKREINVLRRVRHPNIVQLFEVMASKTKIYFVMEYVRGGELFSRVSKGRLREDTARRYFQQLVSAVDFCHARGVFHRDLKPENLLVDENGDLKVSDFGLAAGPDQFDPDGLLHTFCGTPAYVAPEVLRRRGYDGAKADIWSCGVILFALMAGYLPFHDHNIMVLYRKIYNGEFRCPRWFSKDFTRLITRLLDANPKTRITVPEIIESDWFKKGYKPVKFYIEDDKLYNLSDDVLNLEPADPVPPPLGLAPPVPPPPQGDDPDGSGSESDSSVVSCPATLSTGESQRVRGSLPRPASLNAFDIISFSKGFNLSGLFEERGNEIRFVSGEPMSDIVKKLEEIAKVKSFTVRRKDWRVSIEGTREGVKGPLTIGAEIFELTPSLVVVEVKRKAGDNEEYEDFCNMELKPGMQHLVHQMLPAPNGTPVSEKVERSSSLQAPLTLKLIGTEGSMS
|
Involved in drought stress tolerance. CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner.
|
Q5JLS2
|
Q5F788
|
ALR_NEIG1
|
Alanine racemase
|
Neisseria
|
MRPLNVQIRLGNLRHNYRILKEMHGGKLLAVVKADAYGHGAVRCAFALADLADGFAVATIDEGIRLRESGITHPIVLLEGVFEASEYEAVEQYSLWPAVGNQWQLEALLSRHWKKPVKVWLKMDSGMHRTGFFPHDYTSAYAALKQSEYVDSIVKFSHFSCADEPESGMTEIQMEAFDLGTKGLEGEESLANSAAILNIPEARRDWGRAGLALYGISPFGGSDDRLKPVMRLSTRIFGERVLQPHSPIGYGATFYTSKSTRVGLIACGYADGYPRRAPSNSPVAVDGKLTRVIGRISMDMMTIELDASQEGLGHEVELWGDTVNINTVAEAAGTIPYELMCNIKRAKFTYIE
|
Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
|
Q5F788
|
Q21X03
|
RIMO_ALBFT
|
Ribosome maturation factor RimO
|
Rhodoferax
|
MSEVITKSNTAPKVGFVSLGCAKALTDSELILTQLSAEGYQTSKTFQGADLVIVNTCGFIDDAVKESLDTIGEALAENGKVIVTGCLGAKTAEGGGNLVRQMHPSVLAVTGPQATQEVMDAVHANLPKPHDPFIDLVPNAFGVAGIKLTPRHYAYIKISEGCNHRCTFCIIPSMRGDLVSRPIGDVLKEARALFEGGVKELLVISQDTSAYGVDVKYRTGFWDGKPTKTRLLELAAALGDMAEPYGAWVRLHYVYPYPSVDDLLPLMAAGKVLPYLDVPLQHSHPEVLKRMKRPASGEKNLERIQRWREVCPDIVVRSTFIAGFPGETEEEFSHLLDFMREAQIDRAGCFAYSPVQGAVANDIGGMLPIELREERRARFMAVAEAVSSAKLQQRIGATMQVLVDSAPGLGKKGGLGRSYADAPEIDGVVKLLPPEKISKTLRVGEFTKARIVGAQGHDLVAQPF
|
Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12.
|
Q21X03
|
B7J917
|
RS6_ACIF2
|
30S ribosomal protein S6
|
Acidithiobacillus
|
MRHYEIVFLVHPDQSEQVPQMIERYRGMIESDGGHFHRLEDWGRRQLAYPIKKAHKAHYVLMNIECSSVALAELEDAFRFNDAVLRHLILARDEAVTSPSFLARDETDRRERSEETAEGEGEPDHSANEAVVTA
|
Binds together with S18 to 16S ribosomal RNA.
|
B7J917
|
Q9AAF9
|
RL11_CAUVC
|
50S ribosomal protein L11
|
Caulobacter
|
MAKKILGYIKLQVKAGSATPSPPIGPALGQRGVNIMGFCKEFNARTENVEKGTPLPTVITVYQDKSFTFITKTPPATHYLKQITGLKSGAKLTGRETVGEVTRTQLREIAEKKMKDLNANDLEAAAKIIEGSAKAMGLKIVEA
|
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
|
Q9AAF9
|
B0CBF7
|
APT_ACAM1
|
Adenine phosphoribosyltransferase
|
Acaryochloris
|
MDLKSLIRDIPDFPKPGILFRDITTLLQNPDGLRYVIDQFTEDYREQSIDYVVGIESRGFIFGAPLAYQLGAGFVPVRKPGKLPAAIHAQEYELEYGTDRLEIHQDACPAGSRVLVVDDLLATGGTAAATAQLLAPLNCTLVGFGFIIELTGLAGRQKLPDCHINALVEY
|
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
|
B0CBF7
|
Q2YQ02
|
HIS3_BRUA2
|
Phosphoribosyl-AMP cyclohydrolase
|
Brucella
|
MPRFDASGLITAIVTDARDGELLMVAHMNEEALRLTLETGIAHYWSRSRKTLWKKGETSGNLQSVVELRTDCDQDALWLKVHVAGDGPTCHTGRRSCFYRQVVSSGGKVALTMASDHDQ
|
Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
|
Q2YQ02
|
Q87YF5
|
LPXK_PSESM
|
Lipid A 4'-kinase
|
Pseudomonas
|
MALTDRLLDAWYKGHPALTLLRPLESLYRRVVDGKRAKFLAGEGDIYRAPVPVIVVGNITIGGTGKTPLILWMIEHCQRKGLRVGVVSRGYGAKPPSLPWRVQPDQSASEAGDEPLLIVQRSGVPLMIDPDRSRAVQALLAAEPLDLILSDDGLQHYRLARDLELVLIDAARGLGNRRCLPAGPLREPVERLSSVDALLYNGATADRDDGYAFTLKPSALINLRSGERQPVSYFPAGQALHAVAGIGNPQRFFNTLEGLHWRPVTHAFADHALYSVQALTFTPALPLVMTEKDAVKCRAFAADDWWYLAVDAVPSDAFVGWFDEQLLRLSP
|
Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
|
Q87YF5
|
P07429
|
HBB1_XENTR
|
Hemoglobin beta-1 chain
|
Silurana
|
MVNLTAKERQLITGTWSKICAKTLGKQALGSMLYTYPWTQRYFSSFGNLSSIEAIFHNAAVATHGEKVLTSIGEAIKHMDDIKGYYAQLSKYHSETLHVDPYNFKRFCSCTIISMAQTLQEDFTPELQAAFEKLFAAIADALGKGYH
|
Involved in oxygen transport from the lung to the various peripheral tissues.
|
P07429
|
Q06607
|
IHFB_RHOCA
|
Integration host factor subunit beta
|
Rhodobacter
|
MIRSELIAKIAEENPHLFQRDVEKIVNTIFEEIIEAMARGDRVELRGFGAFSVKKRDARTGRNPRTGTSVAVDEKHVPFFKTGKLLRDRLNGGEE
|
This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control. Involved in hydrogenase gene expression.
|
Q06607
|
Q08777
|
MCH5_YEAST
|
Riboflavin transporter MCH5
|
Saccharomyces
|
MSSDSLTPKDTIVPEEQTNQLRQPDLDEDSIHYDPEADDLESLETTASYASTSVSAKVYTKKEVNKGTDIESQPHWGENTSSTHDSDKEEDSNEEIESFPEGGFKAWVVTFGCFLGLIACFGLLNSTGVIESHLQDNQLSSESVSTIGWLFSLFLFVCSASCIISGTYFDRNGFRTIMIVGTVFHVAGLFATANSTKYWHFILSFAIVCGFGNGIVLSPLVSVPAHYFFKRRGTALAMATIGGSVGGVVFPIMLRSFFSMKSDTDPTYGFVWGIRTLGFLDLALLTLSIILVKERLPHVIENSKDGESRWRYILRVYILQCFDAKAFLDMKYLFCVLGTVFSELSINSALTYYGSYATSHGISANDAYTLIMIINVCGIPGRWVPGYLSDKFGRFNVAIATLLTLFIVMFVGWLPFGTNLTNMYVISALYGFCSGSVFSLLPVCCGQISKTEEFGKRYSTMYFVVGFGTLVGIPITGAIISIKTTADYQHYIIFCGLATFVSAVCYIISRAYCVGFKWVRF
|
Riboflavin transporter involved in riboflavin (vitamin B2) uptake. Does not act in the transport of monocarboxylic acids across the plasma membrane.
|
Q08777
|
Q8RFY9
|
PLSY_FUSNN
|
Lysophosphatidic acid synthase
|
Fusobacterium
|
MAFFCFIVLTYFIGAIPSGVWIGKAFKGVDVRDYGSKNSGATNSYRVLGAKLGVAVLIMDVLKGFIPLYIASKFNLVYNDLVILGLVAILAHTFSCFISFKGGKGVATSLGVFLFLIPVITLILLAIFILVAYFTKYVSLASITAAFLLPIFTFFTHKDSYLFALSVIIAVFVIYRHKTNISRLLSGTENKFKF
|
Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
|
Q8RFY9
|
Q9DCE5
|
PK1IP_MOUSE
|
Putative PAK inhibitor Skb15
|
Mus
|
MELVAGSYEQVLFGFTVQRGPAKSGHQETWTPVADFTHHSHTASLSVLASNSRYVVSGSKDETIHIYDMKRKVEHGALVHHAGTVTCLKFHGNQHLISGAEDGHICIWDVKRWKCLKTFKAHRGHVTFLSIHPSGKLALSVGTDKTLRTWNLIEGRSAFIKNIKENAHIVEWSPSGGKYIVVVQNKVDVYRLGTASVSGTITNGKRISSVTFLSDSVLAVAGDEEVVRIFDCDSLECLCEFRAHENRVKDMVSFEVPDHHVLVTASNDGFIKMWTLPQDKKVPPSLLCEAKTGARLTCLTVWLDRAANGMASLPPAAEPCPDQPKTIEKESGDTVQEETSEPNSEKSDVSGDSKQPTKGNSPVTAKKRKMATMSEKKRKKKM
|
Negatively regulates the PAK1 kinase. PAK1 is a member of the PAK kinase family, which has been shown to play a positive role in the regulation of signaling pathways involving MAPK8 and RELA. PAK1 exists as an inactive homodimer, which is activated by binding of small GTPases such as CDC42 to an N-terminal regulatory domain. PAK1IP1 also binds to the N-terminus of PAK1, and inhibits the specific activation of PAK1 by CDC42. May be involved in ribosomal large subunit assembly.
|
Q9DCE5
|
A2BTD0
|
RL16_PROMS
|
50S ribosomal protein L16
|
Prochlorococcus
|
MLSPKRTKFRKQHRGRMRGVASKGNTIAFGQFALQAQDCGWVTARQIEASRRAMTRYIKRGGQIWIRIFPDKPVTMRPAETRMGSGKGNPEFWVAVVKPGRILFEMGGEDITEETAKEAMRLAQYKLPVKTKFISIDKNLENSSQENTKDSKKSQEEVKQ
|
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
|
A2BTD0
|
Q9MUW2
|
PSBD_MESVI
|
Photosystem Q(A) protein
|
Mesostigma
|
MTISIDKSVKKAEPSIFDLCDDWLKRDRFVFIGWSGLLLLPCAYFALGGFFTGNTFVTSWYTHGLASSYLEGCNVLTAAVSTPSNAMGHSLLLLWGPEAQGDFTRWCQLGGLWTFTALHGAFGLIGFMLRQFEIARAVKIRPYNAIAFSGPIAVFVSVFLIYPLGQQSWFFAPSFGVAAIFRFILFFQGFHNWTLNPFHMMGVAGVLGAALLCAIHGATVENTLFEDGDAANTFRAFNPTQSEETYSMVTANRFWSQIFGVAFANKRWLHFFMLFVPVTGLWMSAIGVVGLALNLRAYDFVSQEIRAAEDPEFETFYTKNLLLNEGIRAWMAAQDQPHENLVFPEEVLPRGNAL
|
Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. D2 is needed for assembly of a stable PSII complex.
|
Q9MUW2
|
O60052
|
FNTA_SCHPO
|
Type I protein geranyl-geranyltransferase subunit alpha
|
Schizosaccharomyces
|
MDPIDPELNEILDFTEYGPLTPIPQDDGENPLAKICYTTGYEQGMAYFRAIMAKKEYSLRALNLTGFLIMNNPAHYTVWAYRFQILNHTPSYIDNELEWLDEIAEDFQKNYQVWHHRQKILSLTKNYERELEFTKKMFEIDSKNYHVWSYRVWILQNFNDYSQELKLTNELLEKDIYNNSAWNHRFYVLFETSKVVSWSLEEELNYLKDKILFAPDNQSAWNYLCGVLDKSGPSKLDNLIANLRKNLPALHKPLLEFLAMYEPSSSEEIYQKLANEVDVPHAALWTWMSQRSNP
|
Catalyzes the transfer of a farnesyl or geranyl-geranyl moiety from farnesyl or geranyl-geranyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. The alpha(cwp1) subunit is thought to participate in a stable complex with the substrate. The beta(cpp1 or cwg2) subunits bind the peptide substrate.
|
O60052
|
Q60887
|
OL148_MOUSE
|
Olfactory receptor 7F
|
Mus
|
MDNYTLLNEFILLGIPQTQGLETLLFVVFLFIYFFTLLGNSLIFTAIISSSTLHTPMYFFLGLLSVFDMLFPSVTCPKMLFYLSVRSPAISYKGCAAQLFFYHLLGSTEGCLYSVMAYDRYVAICHPLRYMLIMKPGVCVSLVIIAWLVGCLHATILTSLTFQLVYCASNQVDYFFCDLPAVLPLACTDSKLARKVGSINVGFLALMLLFSVCVSYVHIGVAILRIRSAEGRQKAFSTCSAHLTAILCAYGPVIIIYLQRTPNPLLGAVVQILNNIVSPMLNSLIYSLRNKEVKRSLRRVFQNITFHGQK
|
Odorant receptor.
|
Q60887
|
D2Y2N0
|
H8A17_CYRHA
|
Peptide F4-27.90
|
Haplopelma
|
MVNVKASMFLTFAGLVLLFVVCYASESEEKEFPKEMLSSIFAVDNDFKQEERDCAGYMRECKEKLCCSGYVCSSRWKWCVLPAPWRR
|
Ion channel inhibitor.
|
D2Y2N0
|
B2AG52
|
COAX_CUPTR
|
Pantothenic acid kinase
|
Cupriavidus
|
MNAPRLLVDIGNTRLKWAWCEAGAPLPASTGTTVLPTPWQHAGAVAHAADGALRTLAAELRALRAGGPMPSVWISNVAGPVIAAAVDAALADAFGGCAPVQWVRSAAAHGDLVNGYREPTQLGVDRWVGAVGAHRWLPRDTLLVVTAGTATTLDIVTVAAEGGARFEGGLILPGLALMLGTLARNTAQLPALDVGEAGSVAGAQRRWADNTHDAIAAGCLAAQAGAIERTWRALGERGDAARPPRCLLSGGARGALAGALAVPFEMHDNLVLLGLHAMAMADA
|
Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
|
B2AG52
|
Q8DIB2
|
GCSH_THEVB
|
Glycine cleavage system H protein
|
Thermosynechococcus
|
MTLTYPEDLQYLDSHEYLRLEGDTATLGISAFAVDQLGDIVFVELPAVGDALEPGERFGTIESVKAVEDLYAPLGGTVIAVNQAVIDNPEQIAADPYGEGWLVKVQVSTLPTGLLSAADYRALVEGS
|
The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
|
Q8DIB2
|
A0A068J840
|
UGT1_PANGI
|
UDP-glycosyltransferase 1
|
Panax
|
MKSELIFLPAPAIGHLVGMVEMAKLFISRHENLSVTVLIAKFYMDTGVDNYNKSLLTNPTPRLTIVNLPETDPQNYMLKPRHAIFPSVIETQKTHVRDIISGMTQSESTQVVGLLADLLFINIMDIANEFNVPTYVYSPAGAGHLGLAFHLQTLNDKKQDVTEFRNSDTELLVPSFANPVPAEVLPSMYVDKEGGYDYLFSLFRRCRESKAIIINTFEELEPYAINSLRMDSMIPPIYPVGPILNLNGDGQNSDEAAVILGWLDDQPPSSVVFLCFGSYGSFQENQVKEIAMGLERSGHRFLWSLRPSIPKGETKLQLKYSNLKEILPVGFLDRTSCVGKVIGWAPQVAVLGHESVGGFLSHCGWNSTLESVWCGVPVATWPMYGEQQLNAFEMVKELGIAVEIEVDYKKDYFNMKNDFIVRAEEIETKIKKLMMDENNSEIRKKVKEMKEKSRAAMSENGSSYNSLAKLFEEIM
|
Component of the dammarane-type triterpene saponins (e.g. ginsenosides or panaxosides) biosynthetic pathway . Glycosyltransferase that catalyzes the biosynthesis of ginsenoside F1 from protopanaxatriol (PPT) . Triggers C20-OH glycosylation of ginsenoside Rg3 to produce ginsenoside Rd . Mediates the conversion of protopanaxadiol (PPD) to the ginsenoside compound K . catalyzes the production of 20S-O-beta-(D-glucosyl)-dammarenediol II form dammarenediol II (DM) .
|
A0A068J840
|
Q6YQU0
|
G6PI_ONYPE
|
Phosphohexose isomerase
|
Candidatus Phytoplasma asteris
|
MLKLNLEGIYNFLDWHNYAQTFAPQIKVIHQKLHQDQQLKEKYLGWLELPLHFDFQELEKMKQLKNSHPNLDVLVVIGIGGSYLGAKAGIEFLQTPFKKTKPEILFAGHQASGNYLTNLLHYLKDKNWAINVISKSGITLEPALAFRILKKEIEEKYGKQLAKNRIFVTTDSQKGVLLNLALKEGYQTFVIPDSVGGRFSVFTSVGILPFVFANLDVVSMMKGALQAYHDTFQEDLFQNQAYQYALARYLLHTQQNKKMELLVSYEPHLLSFSEWWKQLFAESEGKEEKGLFVGATNNSTDLHSLGQFIQEGTKMLFETVLNVTSIKDDCVVPHIPNELDNLNYVAGKTYSQINQKILQATKQAHIEGKVPNLEIVIPTLDAYHFGYLAYFFQKACAMSGSLLGINPFNQPGVEIYKQKMFALLKS
|
Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
|
Q6YQU0
|
Q04373
|
PUF6_YEAST
|
Pumilio homology domain family member 6
|
Saccharomyces
|
MAPLTKKTNGKRSAKEVSHSEKKLAKKPRISIDSSDEESELSKKEDAVSSSSDDDDLDDLSTSDSEAEEEADELDISDDSEEHENENEEKEGKDKSEGGENGNHTEQRKLLKERKMQRKSGTQVQQIKSVWERLRVKTPPLPKQIREKLSNEIWELSKDCISDLVLKHDASRIVQTLVKYSSKDRREQIVDALKGKFYVLATSAYGKYLLVKLLHYGSRSSRQTIINELHGSLRKLMRHREGAYVVEDLFVLYATHEQRQQMIKEFWGSEYAVFRETHKDLTIEKVCESSIEKRNIIARNLIGTITASVEKGSTGFQILHAAMREYVKIANEKEISEMIELLHEQFAELVHTPEGSDVACTLVARANAKERKLILKALKNHAEKLIKNEYGNIVFITILNCVDDTVLVFKTFSPTVKEHLQEFIIDKFGRRPWLYILLGLDGKYFSPIVKNELLRYIELSKATSKKDPLQRRHELLSKFAPMFLSTISKDYSSILTENLGCQFIAEVLINDELYAQLNEKDQEKYQQVLNNILTTFKGDITEEEHPIHRAFSTRLLKALIQGGKWNNKEKKVIPLKNVQGLGVPFAEKLYDEIIDSSNLLEWINNADSSFTIVALYETLKDQKEGKPFLKDLRGVQSKITTDESNKGSQLLAKLLK
|
RNA-binding protein involved in post-transcriptional regulation. Component of the ASH1 mRNP which transports the ASH1 mRNA to the distal tip of the bud, where the ASH1 protein is translated and targeted to the daughter cell nucleus. Binds to the ASH1 3'-UTR containing the PUF consensus UUGU segment and represses its translation. This silencing of ASH1 mRNA is critical for asymmetric seggregation of ASH1 to the daughter cell nucleus.
|
Q04373
|
A7ZNS3
|
THIM_ECO24
|
4-methyl-5-beta-hydroxyethylthiazole kinase
|
Escherichia
|
MQVDLLSSAQSAHALHLFHQHSPLVHCMTNDVVQTFTANTLLVLGASPAMVIETEEASQFAAIASALLINVGTLTQLCAQSMCAAVEQAKSSQTPWTLDPVAVGALDYRRRFCLELLSHKPTAIRGNASEIMALAGIANGGRGVDTTDAAANAIPAAQTLARETGAIVVVTGEMDYVTDGHRIIGIHGGDPLMTKVVGTGCALSAVVAACCALPGDTLENVASACHWMKQAGERAVARSEGPGSFVPHFLDALWQLTQEVQA
|
Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
|
A7ZNS3
|
A8GL98
|
RRAA_SERP5
|
Regulator of ribonuclease activity A
|
Serratia
|
MKYDTSELCDIYHEEVNVVEPLFSNFGGRTSFGGQITTVKCFEDNGLLFELLEENGRGRVLVIDGGGSVRRALINAELARLATQNEWEGIVVYGAVRQVDDLEEMDIGIQAMAAIPVGAASESIGESDIRVNFGGVTFFSGDHLYADNTGIILSEDPLDIE
|
Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome. Modulates RNA-binding and helicase activities of the degradosome.
|
A8GL98
|
Q4WXP0
|
NDC80_ASPFU
|
Probable kinetochore protein ndc80
|
Aspergillus subgen. Fumigati
|
MRSDGLRLTNIFLIQTLGSVQNYSALPQPSSALKRTSSIGYQNPPFTSQHTRSMSLLNSASRPQQPNFQRSSSGGAFGADAGLSSVRRSVSSNIFHGASVGRPSYAPGSLSASSASQSLQRRSSVFSRPSVGGPMGHQSFFTQVPNAAGVPRDPRPLRDRSFQARIGQELLEYLTHNNFELEMKHSLGQNTLRSPTQKDFNYIFQFLYHRIDPGYRFQKSMDAEVPPILKQLRYPFEKGITKSQIAAVGGQNWPTFLGMLHWLMQLAQMMDRFVLGEYDEACAEMGVDVSGDRIIFRFLTGAYHDWLQGGEDEDDETAEKRLVPHIESMAQEFERGNEKYMQEMQVLEAENRALRDQIEELEKNAPDMAKLDKHFRILEDDKRKFEDYNQNVQGKIEKYENRIKFLEEEIQKVEAELQAAEEERSSLQSSVDQQGITIQDIDRMNTERDRLQKSLEDTTARLEETHARVMEKEAEASRKLEDLEEIVKVYNTLGYQTSLIPSTAVNAKGQDYELSLNINDNSFSASQIGGLPNRISSEADRLLAEPFTGYHPAHLLNLDLRGMVRSSLQALRKEINERRKRAIDDDLERRNLLDNIKEAMDEKRSEVEALEHKRRAAEEEFERLKEITTTQKLASDAQIEKMEKELAKMRATLSESVQLMEQREMNTNIEYEQLTLRANALREELHTNVESMLNDVIRFKVHIQKGLEDYESFVVDEVEQELGGDLPATKDVTSQT
|
Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity.
|
Q4WXP0
|
Q7N227
|
HSCB_PHOLL
|
Hsc20
|
Photorhabdus
|
MDYFTLFGLPARYTVDREQLASCYQELQRQFHPDRFASQPEREKTLALQQAVTINDGYQTLKHPLKRAEYMLSLHGFDLANEQHTMNDNAFLMEQLMLREELECIADKANPEVALADFAARLNGMIKTRSQLMVQQLDEQQWEQAADTVRKLRFLDKLQQQVEQLEERLLDDF
|
Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA.
|
Q7N227
|
Q8PKS0
|
UVRC_XANAC
|
Excinuclease ABC subunit C
|
Xanthomonas
|
MSVRPQNDFDGKAFAAQLSTAPGVYRMYAGDDTLLYVGKAGALRKRVGSYFNGTPKNARLTSMLSQVARMDVTVTRSEAEALLLENQLIKSLSPRYNVSLRDDKSYPYVLLTREQWPRIALHRGPRAVQGRYFGPYTGVTGVRETLSLMHKLFKLRSCEDSVFRNRSRPCLQYQIGRCSGPCVDLVAAPDYAESVRRATMFLEGKSDQLGEEIMHSMQQASEALEFERAARLRDLLSSLRSMQNRQYVDGRAADLDVLACATQSSQACVLLLSFRDGRNLGTRSFFPKTNGEDSADEILGAFVSQYYAEHSPPREILLDREIPEAELIEAALSTAAEHKVALKWNVRGERAGYLLLATRNAQLTLVTELTSQSAQHARSEALRELLGLAEPVKRVECFDISHTMGEATVASCVVFDASGPVRGQYRRFNISGITPGDDYAAMRQAIERRFRRAVEENGVIPDVLLIDGGAGQLAQAQAALADLGVENVLLVGVAKGEERRAGHEALIMADGRELRPGAASPALQFIQQVRDEAHRFAITGHRGRRQKARMTSKLEDIPGIGPRRRASLLKHFGGLVGLKAAGEAEIARVEGVNAALAARIYANLHGLALPDAAGEASPQ
|
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.
|
Q8PKS0
|
B5XNA9
|
RL18_KLEP3
|
50S ribosomal protein L18
|
Klebsiella
|
MDKKSARIRRATRARRKLQELGATRLVVHRTPRHIYAQVIAPNGSEVLVAASTVEKAISEQLKYTGNKDAAAAVGKAVAERALEKGIKDVSFDRSGFQYHGRVQALADAAREAGLQF
|
This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
|
B5XNA9
|
Q74JV6
|
COAD_LACJO
|
Pantetheine-phosphate adenylyltransferase
|
Lactobacillus
|
MIKAIFPGSFDPITNGHVEVIEGASHMFEKLYVVIMTNTSKKYLFTEKERLELARKVFENNEKVEVIARPAELTVEVAHELGAGAIVRGLRNTADFNYERDIAGINKTLDPDLNTVLLFTRPEDSFISSSMIKETVFFGGDVSTLVPKPVAAALEEKLRNRNNEKK
|
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
|
Q74JV6
|
A2C210
|
PETN_PROM1
|
Cytochrome b6-f complex subunit VIII
|
Prochlorococcus
|
MIFTLGWASLAAIFTFSIAMVVWGRNGDGSIDL
|
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
|
A2C210
|
Q12RW2
|
ALR_SHEDO
|
Alanine racemase
|
Shewanella
|
MKPFPRAEISRKALQANLARIRELAPQSKIMAVVKANGYGHGLLNVANSVATYDQGADGFGLARLEEALELRSGGVNARLLLLEGFFRVTDLPLLVQHHIDTVVHHESQVEMLEQAELTTPVTVWMKIDTGMHRLGFSLAQFDAIYQRLLACHNIAKPIHLMTHFACSDEPDNSFTQAQIDAFESVTASLDGDRSLANSGGMLFWPQSQRDWIRAGIALYGVSPMVGDKGGNHGLVPAMELKSQLISVKDHQAGDSVGYGAFWRARKDTRIGVVAIGYGDGYPRHAPEGTPVWLNGRRVPIVGRVSMDMLTVDLGLDSQDKVGDEVLLWGSALAVEEVADHIGTIAYELVTKLTPRVAVALLP
|
Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
|
Q12RW2
|
P01938
|
HBA_LORTA
|
Hemopressin
|
Loris
|
VLSPADKTNVKTAWEKVGGHAGEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKAHGKKVADALTTAVSHVDDMPSALSALSDLHAHKLRVDPVNFKLLSHCLLVTLACHHPADFTPAVHASLDKFLASVSTVLTSKYR
|
Hemopressin acts as an antagonist peptide of the cannabinoid receptor CNR1. Hemopressin-binding efficiently blocks cannabinoid receptor CNR1 and subsequent signaling.
|
P01938
|
Q37D32
|
RBL2_RHOPS
|
Ribulose bisphosphate carboxylase
|
Rhodopseudomonas
|
MDQSNRYANLNLKESDLIAGGRHVLCAYIMKPKAGFGNFVETAAHFAAESSTGTNVEVSTTDDFTRGVDALVYEVDEAKELMKIAYPIELFDRNVIDGRAMIASFLTLTIGNNQGMGDVEYAKMHDFYVPPAYLRLFDGPSTTIKDLWRVLGRPVVDGGFIVGTIIKPKLGLRPQPFADACYDFWLGGDFIKNDEPQGNQVFAPFKDTVRAVNDAMRRAQDATGQPKLFSFNITADDHYEMLARGEYILETFGENADHVAFLVDGYVAGPAAVTTARRAFPKQYLHYHRAGHGAVTSPQSKRGYTAFVLSKMARLQGASGIHVGTMGYGKMEGEASDRDSAFMITQDSAEGPYFKQEWLGMNPTTPIISGGMNALRMPGFFANLGHSNLIMTAGGGAFGHIDGGAAGARSLRQAEQCWKQGADPVAFAKDHREFARAFESFPNDADKLYPNWRNMLKLAAA
|
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site.
|
Q37D32
|
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