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2.75k
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AlphaFoldDB
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B6H2I7
RSSA_PENRW
40S ribosomal protein S0
Penicillium chrysogenum species complex
MAPSQLPPVFNPTAQDIEMLLAAQCHLGSKNLQVHMEPYLWKLRADGVNVLNIGKTWEKIVLAARIIAAIDNPADVCVISARPYGQRAVLKFASHTGATAIAGRFTPGNFTNYITRSFKEPRLIIVTDPRTDAQAIKEASYVNIPVIALCDTDSPTDFVDVAIPTNNKGRHAIGLVWWMLAREVLRLRGTLATRETEWDTVVDLYFYRDPEAEENKEIADESKVAGAEEIGAGAVESGFAGENWDASAPGAGNPGTAFAAASAATGAAAATSWDAEGADWAASSAAPTTEWAEAQPAAGEAKW
Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits.
B6H2I7
A3CMR7
THII_STRSV
tRNA 4-thiouridine synthase
Streptococcus
MQYSEIMVRYGELSTKGKNRMRFINKLKRNIQAVLSVYPKVHVKADRDRTHVYLHGTDYQPVAESLKQIFGIQNFSPSYKIEKSVPALIEAVQSIMKEVYQEGMTFKITSKRSDHSFELDSRELNQTLGDAVFEAIPNVQVKMKAPDIELRVEIREEAAYISYETIRGAGGLPVGTSGKGMLMLSGGIDSPVAGYLALKRGVDIEAVHFASPPYTSPGALKKAQDLTRKLTKFGGNIQFIEVPFTEIQEEIKAKAPEAYLMTLTRRFMMRITDRIREERSAQVIINGESLGQVASQTIESMQAINAVTNTPVIRPVVTMDKLEIIDIAEKIDTFQISIQPFEDCCTIFAPDRPKTNPKIKNAEKYETYLDVEGLVERAVAGIMITEITPQAETDEVDELIEGLL
Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
A3CMR7
B2HME9
PROA_MYCMM
Glutamyl-gamma-semialdehyde dehydrogenase
Mycobacterium
MTLQAAPRSAAAQQREPDLRQEVHDAARRARVAARLLAVVPTGVKDRALHAAADAILAHVDRILSANAEDLDAARAADTPAAMLDRLALNPQRVDGIAAGLRQVAGLPDPVGEVLRGYTLPNGLQLRQQRVPLGVVGMIYEGRPNVTVDAFGLTLKSGNAALLRGSSSAARSNEALVNVLRSALDSEQLPADAVQLLSSADRSTVTHLIQARGLVDVAIPRGGAGLIDAVVRDAQVPTIETGVGNCHVYVHEAADLDVAERILLNSKTRRPSVCNAAETLLVDAAIAEHAMPRLIGALQDAGVTVHLDADEQDLRREYLAMEIAVAVVDGVDGAIAHINEYGTGHTEAIVTTNLAAAQRFTERIDAAAVMVNASTAFTDGEQFGFGAEIGISTQKLHARGPMGLPELTSTKWIVWGEGHTRPA
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.
B2HME9
Q1QN15
RL6_NITHX
50S ribosomal protein L6
Nitrobacter
MSRIGKRPVTVPSGVTATVEGQTVRMKGPKGQLEFVVHNDVEVKLENGAVKVAPRYETNRAQALYGTARAQVANLVAGVTKGFEKKLEIVGVGYRAALQGKTLQLALGYSHDVSYAIPEGITIAVPKPTEITIAGNDAQRVGQVAAEIRGYRPPEPYKGKGVKYADEFIFRKEGKKK
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.
Q1QN15
Q45538
COTJC_BACSU
Protein CotJC
Bacillus
MWVYEKKLQYPVKVSTCNPTLAKYLIEQYGGADGELAAALRYLNQRYTIPDKVIGLLTDIGTEEFAHLEMIATMVYKLTKDATPEQLREAGLGDHYVNHDSALFYHNAAGVPFTASYIQAKGDPIADLYEDIAAEEKARATYQWLIDISDDPDLNDSLRFLREREIVHSMRFREAVEILKEERDKKKIF
The cotJ operon proteins affect spore coat composition. They are either required for the normal formation of the inner layers of the coat or are themselves structural components of the coat.
Q45538
Q00GL7
PSBU_KARBR
PSII-U
Karenia
MQKMAMLMACLACMGLAAAFSPATLGVNKPSHRQQAPVMSQVARRELLSKVLGAAALLGAASADAKVNYDAVAYLGGAQQIDVNNANIRVYQKLPGMYPSAAGKLCTNGPYVDLKDMYAKAKLSKEEEAIVKEFDKDFLFLKPQIEYVVDNLNNGLYRR
Stabilizes the structure of photosystem II oxygen-evolving complex (OEC), the ion environment of oxygen evolution and protects the OEC against heat-induced inactivation.
Q00GL7
C5BEW3
AROQ_EDWI9
Type II DHQase
Edwardsiella
MADKFNILLLNGPNLNMLGVREPEKYGTLTLAQIAARLDRRAQALGVSLHHIQSNAEHELIAQIHAAFGNTDFILVNPAAFTHTSVALRDALLAVQIPFIEIHLSNVHAREPFRHHSYLSDIAVGVICGLGAEGYEYALQAAVNRLNKS
Catalyzes a trans-dehydration via an enolate intermediate.
C5BEW3
Q8YAA3
RL7_LISMO
50S ribosomal protein L7/L12
Listeria
MALNIEEIIASVKEASVLELNDLVKAIEEEFGVTAAAPVAVAAAGGAAAEQTEFTVELASAGDSKIKVIKVVREITGLGLKEAKELVDNAPKALKEGIAKDEAEEIKAKLEEVGANVEVK
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
Q8YAA3
A3DF25
DNAK_ACET2
Heat shock protein 70
Acetivibrio
MGKVIGIDLGTTNSCVAVMEGGEPVVIPNSEGSRTTPSVVAFTKNNERLVGQVAKRQAITNPERTIISIKRDMGTDKRVKIDDKSYTPQEISAMILQKIKADAEAYLGEKVTQAVITVPAYFSDSQRQATKDAGRIAGLEVLRIINEPTAAALAYGLDKESDQKILVFDLGGGTFDVSILEIGDGVFEVLATSGNNRLGGDDFDQRIIDYLIDLFKKEHGIDLSTDKMAMQRLKEAAEKAKIELSGVTTTNINLPFITADANGPKHLDVTLTRAKFEELTADLVEKTMEPTRRALEDSGLTPDKIDKILLVGGSTRIPAVQEAVRKFFGKEPFKGINPDECVAIGAAIQAGVLTGEVKDLLLLDVTPLSLGIETLGGVFTKLIERNTTIPTKKSQIFSTAADGQTAVTVRVFQGERAMAADNKLLGEFTLDGIPPAPKGVPQIEVTFDIDANGIVHVSAKDLGTGKEQHITITASTNLSEAEIEKAINEAKKYEEEDRKRKESAETRNNADSMVFQAEKTLKDLGDKLSSEDKAKIEAEIEKVREALKGTDTQAIKKATEDLQQAFYSVSAKIYQQGQAAGANPGAQTTGGEQGNVYDAEYKVVDDDK
Acts as a chaperone.
A3DF25
A7H101
RL24_CAMC5
50S ribosomal protein L24
Campylobacter
MANVKFQVKKGDLVKIIAGDDKGKTGKILSVLAKKSQVIVEGCKVAKKAIKPSEKIPNGGHINKEMPIHISNVAKVEE
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
A7H101
Q28NC3
IF1_JANSC
Translation initiation factor IF-1
unclassified Jannaschia
MAKEEMLEFPGVVKELLPNATFRVELENGHEIIAHTAGKMRKNRIRVLAGDKVQVEMTPYDLTKGRINYRFK
One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.
Q28NC3
Q32RY9
ATPE_STAPU
F-ATPase epsilon subunit
Staurastrum
MTLNLRVMAPNRIVWNSEAQEIILSTNSGQIGILPNHAPLLTALDIGVMKVRINSDWCTMALMGGFAMIENNQLTILVNEAEKGSDINLEEAQQTFDLAQESLNQATGKKQTIEANLAFQRAKARLEAVKANSSSAYN
Produces ATP from ADP in the presence of a proton gradient across the membrane.
Q32RY9
Q2P4M4
LEPA_XANOM
Ribosomal back-translocase LepA
Xanthomonas
MSSDSMRNIRNFSIIAHVDHGKSTLADRIIQLCGGLQAREMEAQVLDSNPIERERGITIKAQSVSLPYTAKDGQVYHLNFIDTPGHVDFSYEVSRSLAACEGALLVVDAAQGVEAQSVANCYTAVEQGLEVVPVLNKIDLPTADVDRAKAEIEAVIGIDAEDAVAVSAKTGLNIDLVLEAIVHRIPPPAPRDTDKLQALIIDSWFDNYLGVVSLVRVMQGEIKPGSKILVMSTGRTHLVDKVGVFTPKRKELSALGAGEVGWINASIKDVHGAPVGDTLTLAADPAPHALPGFQEMQPRVFAGLFPVDAEDYPDLREALDKLRLNDAALRFEPESSEAMGFGFRCGFLGMLHMEIVQERLEREYNLNLISTAPTVVYEVLKTDGSVIPMDNPSKLPPLNNVEEIREPIIRANILTPPDYVGNIITLCEEKRGSQIGINYLGSQVQISYELPMAEVVLDFFDKLKSVSRGYASLDYHFLRFDPGPFVRVDTLINGDKVDALSIIVHRSYADRRGRELCEKMKDLIPRQMFDVAIQAAVGSQIISRSTVKAMRKNVLAKCYGGDVSRKKKLLEKQKEGKKRMKQVGRVEIPQEAFLAVLQMDK
Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.
Q2P4M4
P05695
PORP_PSEAE
Outer membrane protein D1
Pseudomonas
MIRRHSCKGVGSSVAWSLLGLAISAQSLAGTVTTDGADIVIKTKGGLEVATTDKEFSFKLGGRLQADYGRFDGYYTNNGNTADAAYFRRAYLEFGGTAYRDWKYQINYDLSRNVGNDSAGYFDEASVTYTGFNPVNLKFGRFYTDFGLEKATSSKWVTALERNLTYDIADWVNDNVGTGIQASSVVGGMAFLSGSVFSENNNDTDGDSVKRYNLRGVFAPLHEPGNVVHLGLQYAYRDLEDSAVDTRIRPRMGMRGVSTNGGNDAGSNGNRGLFGGSSAVEGLWKDDSVWGLEGAWALGAFSAQAEYLRRTVKAERDREDLKASGYYAQLAYTLTGEPRLYKLDGAKFDTIKPENKEIGAWELFYRYDSIKVEDDNIVVDSATREVGDAKGKTHTLGVNWYANEAVKVSANYVKAKTDKISNANGDDSGDGLVMRLQYVF
Anion specific, the binding site has higher affinity for phosphate than chloride ions. Porin O has a higher affinity for polyphosphates (tripolyphosphate and pyrophosphate) while porin P has a higher affinity for orthophosphate.
P05695
P27424
MFAP2_BOVIN
Tropoelastin-binding protein
Bos
MRAASLFLLFLPAGLLAQGQYDLDPLPPYPDHVQYTHYSEQIENPDYYDYPEMTPRPPEEQFQFQSQQQVQQEVIPAPTLEPGTVETEPTEPGPLDCREEQYPCTRLYSIHKPCKQCLNEVCFYSLRRVYVVNKEICVRTVCAQEELLRADLCRDKFSKCGVLASSGLCQSVAAACARSCGGC
Component of the elastin-associated microfibrils.
P27424
Q9NS85
CAH10_HUMAN
Cerebral protein 15
Homo
MEIVWEVLFLLQANFIVCISAQQNSPKIHEGWWAYKEVVQGSFVPVPSFWGLVNSAWNLCSVGKRQSPVNIETSHMIFDPFLTPLRINTGGRKVSGTMYNTGRHVSLRLDKEHLVNISGGPMTYSHRLEEIRLHFGSEDSQGSEHLLNGQAFSGEVQLIHYNHELYTNVTEAAKSPNGLVVVSIFIKVSDSSNPFLNRMLNRDTITRITYKNDAYLLQGLNIEELYPETSSFITYDGSMTIPPCYETASWIIMNKPVYITRMQMHSLRLLSQNQPSQIFLSMSDNFRPVQPLNNRCIRTNINFSLQGKDCPNNRAQKLQYRVNEWLLK
Does not have a catalytic activity.
Q9NS85
P39734
HPH2_YEAST
High pH protein 2
Saccharomyces
MQNAQIKSSSKGSGIDGTDRNSKDGVEKRPLEDVKQMIDAGTPDVGHKSTVETKPNVGWQASHSNLAALHEKEQKYEMEHHHARHKLHRQVIPDYTSASTAMFSDCMFNAAPDKVRSLSTMKSSGLSPKHPFNVVATFKGPFPQHSVESKPLDGGYSAKDHFPSFKMLQAQQHPAHRHYKDNDKYGLKSPSRSFVKDKKRLVHRFLKSMEPSSSGQSKDSSALAPAFDPILPNVISKPSKRPTHHSHSSDGSSSTQTDISLQSLLYHDLESSPKKHVSPSRPPSVASESSPAVANPIGLSPKDACNASFSQSSSSSLSSSSSSSSSTSFSQSVAVDPLEPPGNITYSSSNLSLNSDELDYYQRHIGLQLQQTEALLKHSLKDEVLKDENDLVKNIANFDKIVKELRDLRSRTIGWKELVEEDYLMNLKQDFDKENPESFEARLSDTINTNVAKLQDLEKRMASCKDRLASRKEVMRKMESLLSLENSLMISKKNVTFASKYRNEALDIVFLIIIIVICYTFKHLVSHK
Required for growth under high NaCl, alkaline pH and cell wall stress.
P39734
Q5E4T4
DNAK1_ALIF1
Heat shock protein 70 1
Aliivibrio
MGKIIGIDLGTTNSCVAVLDGDTPRILENAEGERTTASVIAYTDGETLVGQPAKRQAITNPQNTLFAIKRLIGRRFEDEEVQRDIEIMPYKIIKADNGDAWVEAKGQKMAAPQVSAEILKKMKKTAEDFLGEEVTGAVVTVPAYFNDAQRQATKDAGRIAGLDVKRIINEPTAAALAYGLDKKGGDRTIAVYDLGGGTFDISIIEIDNVDGEQTFEVLATNGDTHLGGEDFDNRLINFLVDEFKKEQGFDLKNDPLAMQRVKEAAEKAKIELSSAQQTDVNLPYVTADATGPKHMNIKVTRAKLESLVEDLVVRTLEPLKVALADADLTIDGITDVILVGGQTRMPMVQAKVAEFFGKEARRDVNPDEAVAMGAAVQGGVLAGDVKDVLLLDVTPLSFGIETMGGVMTKLIEKNTTIPTKADQTFSTAEDNQSAVTIHVLQGERKQASYNKSLGQFNLEGIQAAPRGMPQIEVTFDLDADGILNVSAKDKSTGKEQKITIQASGGLTDEEIEAMVQEAEANKDADKKFEELVTARNQADQMIHGTKKQIEEAGDDLPTDEKEKIEAAITALEGVKSGDDKEAIDAKTQELMQAAQKLMEIAQQKAQAQQGAQAGEQPKQEDDVVDAEFEEVK
Acts as a chaperone.
Q5E4T4
O03889
COX2_APTAU
Cytochrome c oxidase polypeptide II
Apteryx
AICSLVLYLLTLMLMEKLSSNSVDAQEVELVWTILPAIVLILLALPSLQILYMMDEIDEPDLTLKAIGHQWYWTYEYTDFKDLSFDSYMIPTSELPLGHFRLLEVDHRVVVPMESPIRVIITAGDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESTPLPHFENWSSLLSTSSSL
Component of the cytochrome c oxidase, the last enzyme in 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. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
O03889
Q8LGD1
SP1L5_ARATH
Protein SPIRAL1-like 5
Arabidopsis
MSRGGSFGGGQSSLGYLFGSDNEIPKTPAPPVAPKPAPPYGVDSTEEDHEADQKPKISNNNYQRVQGQNSGNFVTDRPTTKVKSVPGGGSSLGYLFGDK
Acts redundantly with SPR1 in maintaining the cortical microtubules organization essential for anisotropic cell growth.
Q8LGD1
Q5PGK9
MACB_SALPA
Macrolide export ATP-binding/permease protein MacB
Salmonella
MTALLELCNVSRSYPSGEEQVAVLKDISLQIHAGEMVAIVGVSGSGKSTLMNILGCLDKPTSGTYRVAGRDVSTLDPDALAQLRREHFGFIFQRYHLLSHLTAAQNVEIPAVYAGIERKKRQARARELLLRLGLSDRVDYPPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILRQLRDRGHTVIIVTHDPLIAAQAERIIEIHDGKIVHNPPAQEKKREQGVDAAVVNTAPGWRQFASSFREALSMAWLAMAANKMRTLLTMLGIIIGIASVVSIVVVGDAAKQMVLADIRAMGTNTIDIHPGKDFGDDNPQYRQALKYDDLVAIQKQPWVNSATPSVSKSLRLRYGNIDIAVNANGVSGDYFNVYGMSFREGNTFNAVQQQDRAQVVVLDANTRRQLFPNKANVVGEVVLVGNMPVIVIGVAEEKPSMYGNSNLLQVWLPYSTMSDRIMGQSWLNSITVRVKDGVDSDQAEQQLTRLLTLRHGKKDFFTWNMDSVLKTAEKTTYTLQLFLTLVAVISLVVGGIGVMNIMLVSVTERTREIGIRMAVGARASDVLQQFLIEAMLVCLVGGALGISLSMFIAFMLQLFLPGWEIGFSLTALASAFLCSTFTGILFGWLPARNAARLDPVDALARE
Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.
Q5PGK9
B1LZY1
URED1_METRJ
Urease accessory protein UreD 1
Methylobacterium
MHGPLAPAPSPERLGAAPARQRSDGRIRLRVGPARPGGGTRILDLAEAGPSRLRFPRGTCALEAVLVNTAGGVACGDSFAIDLALEPGADLVLTTTAAEKIYRSDGPVSRIANTLTLGEGAGLAWLPQETILFDRARVRRRFEADLADGAALIAAEVVAFGRAARGERIVDGLFADSWRIRRGGRLAYADSVLLEGPISDHLARPAIGGGARACATILDVSPGAEARLEEARARLAEAASPGTTAAASAWNGHLAVRALGDAVGPLRGLVARFLAGYRALPMPRVWQS
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
B1LZY1
Q5VJ52
CYB_ALLTR
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
Cheirogaleus
MTNIRKIHPLMKVMNNSFIDLPAPSNISSWWNFGSLLGACLAIQIITGLFLAIHYTADTMTAFSSVSHICRDVNQGWTIRYLHANGASMFFLCLFIHVGRGMYYGSFTLPETWNIGIILLFTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTSLVEWIWGGFSVDKATLTRFFAFHFILPFIIAALVMIHLLFLHETGSNNPLGIASESDKIPFHPYYTIKDLLGLLLLLLLLMTLVLFFPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALITSILILTIIPMLHTAKQRSMTFRPLSQIMFWILTADLSTLTWIGGQPVEHPFIYIGQTASILYFSLILIIIPTVSLMENKMLKW
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.
Q5VJ52
A1K3D3
RL9_AZOSB
50S ribosomal protein L9
Azoarcus
MQIILLEKVVNLGNLGDVVKVKDGYARNFLIPQGKAKRANQANLAEFEARRAELERQQAEKLAAAQEVGAKLEGLMVQIARKAGMDGRLFGSVTNADVAEALAAQGFEIERSTVRMPDGPLKQIGDTQLEVALHSDVVVSITVSVLGEQQQ
Binds to the 23S rRNA.
A1K3D3
Q30Z36
RS12_OLEA2
30S ribosomal protein S12
Oleidesulfovibrio
MPTINQLIRKERKKVAKRKKTPALQACPQRRGVCTRVYTTTPKKPNSALRKVARVRLTNAIEVTAYIPGEGHNLQEHSVVMIRGGRVKDLPGVRYHIVRGTLDTAGVQDRRQGRSKYGAKRPK
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
Q30Z36
Q83GN4
MRAY_TROWT
UDP-MurNAc-pentapeptide phosphotransferase
Tropheryma
MIAILLAVAFGITFTLFTTPFFIRLFRKIGWGQFIRLDGPRQHAIKRGTPTMGGLVIVVASIISYFLANFFLGLSVEPSGLLVIFMFVGMSLVGFLDDILKVRKQHSGGLGPFYKVVLQSFIAVPFALLTFLVKDARGIPHSSMSISFARDTGINFSALFSLGIIGVFSAWILYLLWINLIAVSSVNAVNITDGLDGLAAGAMIFTMLAYVVIGFWQSGQNCARKSLPLENISKCYSVNGPLDMSILAAAILGSLLGFLWWNTNPSKIMMGDTGALALGGAAAALSILTHTQLLFLVLGGLFVIEAGSVILQIAFYKKYRRRIFLMSPLHHHFELKGWAEITVVVRFWIIAGLFTALGIGLFYADWLYS
Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
Q83GN4
A9BA66
AROB_PROM4
3-dehydroquinate synthase
Prochlorococcus
MNQNSIRIKIKLAHNPYEVVIKKNGLARIGEELKKIGFKKATKVLVVTNKDVSVHYGKEFIHNLSDNGFNPTLIEIKAGEERKNLATISDIHNAAYTSRLERGSLMIALGGGVIGDMTGFAAATWLRGVSFVQVPTTLLAMVDASVGGKTGVNHPKGKNLIGAFHQPKLVLIDPITLKTLPEREFKAGMAEVIKYGVISDKKLFRKLEDAPRLDKLETLTDRFLLEIIQRSVQTKAHIVELDEREGGIRAVLNYGHTFGHAIEALCGYGTWLHGEAVSMGMIAIGQLALERNIWNISDLERQRKVLCQAGLPTIWPRVCAEDVIEILKSDKKVKDGEINFIVPTEIGKVEIIKNFTVNEIKQALQKLASK
Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
A9BA66
P62392
HIS3_LEPIC
Phosphoribosyl-AMP cyclohydrolase
Leptospira
MSSREITILKIQEPTRSIASLTRIMEEELSQYRKTLPKGFREEVDCDEDTVLFLHVDFLPLDFQKTTELLLTGKKDLVPVVAIDLQGQILMQAFGNEESQTLSLKTGYAHYFSRSRNQLWKKGDTSGHTQKILQILSPTDRSFLVYQVEQEVAACHEGYYSCFFRERMEGVTWKLLPVPRNFLPEKS
Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
P62392
P84030
CYC2_CERCA
Cytochrome c-2
Ceratitis
MGVPAGDVEKGKKLFVQRCAQCHTVEAGGKHKVGPNLHGLIGRKTGQAAGFAYTDANKAKGITWNEDTLFEYLENPKKYIPGTKMIFAGLKKPNERGDLIAYLKSATK
Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
P84030
Q749L1
CYCC_GEOSL
Polyheme membrane-associated cytochrome c
Geobacter
MSRKVTKYSAVLAVSLFAAALAGCGSENKEGTVGTGPGGVATVGDTACVQCHSAVVDPLTGESIITQYTRSFHYSKGVGCEGCHGGGAQHNGVGPLPFPLAGQSEAQIAARCASCHNGVIAPLSSSPNFVNGNHANPFGGEEAKENLCSRCHSHEGAIFGAQAGFTGDGNILRNAAYQPVYPQDPETFNVMTCATCHQHGGAQRQVFTQISTAGVPNSRRTVAWDPNRNSINDQYDLCTSCHTVNTMTGTLIGSGNVLQIFTSNAVGSGTKSVTTAPFYHNTRWFRTLPSTHYDFPESKTTASGTTIEGYVIRRNTANPCFDCHGHEFQTNTRRLAGADRPNTIFLDWGQSAHGGKLLQAKVAAAALASSGAAEVDDVMKAGATDATAPGWTHYNWDDTASRGACQRCHTSTGASNFLNNPAGYDRTGAGNSFTHLAGWTSSNKRSDQNELLYCWGCHTKAGTGELRNPGAITEVYPGINSTSTGTTGLDVTVSYPDIKGSNVCMGCHLGREVGDNIKAITDADGILGFVNSHYLTAGGQLFGTTGYEYATRSYANPAFFQHDKIGTAAAPGTGTNGPCAGCHMTTPTSHLFLPVTKDGTGAITAITSTACVTCHAGTFALTPEGLTAEEEEYVASLEALKAALAGKGILFFNAHPYFYRDTNANGIADPGETVSSNAFTNWAGVYGLALWQDVMGAAFNANLLIHDPGGYAHNRFYSKRLIWDSIDFIFDGVLNNDVTAAIDAQVTAARLDSATATAAKAYLGATRP
Not involved in Fe(3+) reduction.
Q749L1
Q9JHK4
PGTA_MOUSE
Rab geranylgeranyltransferase subunit alpha
Mus
MHGRLKVKTSEEQAEAKRLEREQKLKLYQSATQAVFQKREAGELDESVLELTSQILGANPDFATLWNCRREVLQQLETQKSPEELAALVKAELGFLESCLRVNPKSYGTWHHRCWLLSRLPEPNWARELELCARFLEADERNFHCWDYRRFVAAQAAVAPAEELAFTDSLITRNFSNYSSWHYRSCLLPQLHPQPDSGPQGRLPENVLLRELELVQNAFFTDPNDQSAWFYHRWLLGRAEPHDVLCCLHVSREEACLSVCFSRPLIVGSKMGTLLLTVDEAPLSVEWRTPDGRNRPSHVWLCDLPAASLNDHLPQHTFRVIWTGSDTQKECVLLKGHQECWCRDSATDEQLFRCELSVEKSTVLQSELESCKELQELEPENKWCLLTIILLMRALDPLLYEKETLEYFSTLKAVDPMRAAYLDDLRSKFLVENSVLKMEYADVRVLHLAHKDLTVLCHLEQLLLVTHLDLSHNRLRALPPALAALRCLEVLQASDNVLENLDGVANLPRLRELLLCNNRLQQSAALQTLASCPRLVFLNLQGNSLCQEEGIRERLAEMLPSVSSILT
Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A.
Q9JHK4
Q7VI80
ACP_HELHP
Acyl carrier protein
Helicobacter
MDTFESVKAVVVEQLSVDANEVKPESRFIEDLNADSLDVVELVMALEEKFSIEIPDEEAEKIKTVKDVVAYIEANK
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
Q7VI80
A8N5E6
PRM1_COPC7
Plasma membrane fusion protein PRM1
Coprinopsis
MSFLTTPPNEHTTLTSYLQLPHLLSLTWLAYPILSLIFVAFRLQASLASSEDAISSAKSNLLASCKAAEEAATSTASLPRYMAIATNQQVADAVNATLRGARAALILTLTVMEAIINFIIDLYRSIFLCFLELVVRGGIAILVGAVEEINNVLATVTSGLRTQIQASVGTLNNALRETIEGINRINPFGDIPVPTFDPPNLDGLDNVSLPDSFQESLLRLNDTIPTVSTIKEKLQDIIGTPFELVKRDINDTFAAVSFSADTLPVPEQNKVSFCSDLDLSVVDDVGNDIVKSAKIGIVILLVIALVLIGLNCLFTWYKWRCMQAHLEYTRQAWNTDPTMQTKGSISATPQIALSNHNLMVLQANSEHPLVTRITNQLSQKLRLSPRTHTHMQWFFNYIFHPPAAACLLIGVFGLLLIEIQLLAMGPLVNKYQEQAAETTKDFSLLIANSINESMLNQSTIYAAEINGRVDSVQTTINDGLFGWVDGTIVPLNTTINEFYDDIQNAVQTVFGGTILETAATEFIRCLIGSKVDAVENALTFLHENLRVDMPRVNDTALMLSPESVNEASAPIAAAAMGGGTDDDQGLIGRLVNSYADSLRKERVTFGIFLALWGVVVLMGLFVLFWHSTGKPLLEKRRRRKYEKSKGMLPEGGFVVPYRDGSAPPSRDEKNLGGGGNGGVGLAMTGDELPQFTPLPSPRRSAFKPFWNPAKPDASGEAKDVEKEPSPMAQVAADEVSKLKAFRLKLMGKSTESLDADSKASDNPPGLFGKVKGVFGKKDADQAPDYWTSYNASSDTVNANTARPNIRVIVDTDQDREDTYGNSFRHSADIEGADIYTPPPNSRWSTSPGPTKTSWNLKKLTLLSPKSSNNKKLPAVSGSSSIGPIPPSMSAAASGLKRQPSVPTDIGASFDDPFMASVSVPRKPSPIVPGIYPVPLHAAAPAINNNPYQRAPSPPKRFVAPYLNDPSALSRNTSGSSASKTHRRSSSHPAAVWRVTNAASTDRLTASPMSSQVSLPARMLTSENPFITPFDDEHRVEVVNPSRGEVRKSMAVNPFSNAAAVAI
Involved in cell fusion during mating by stabilizing the plasma membrane fusion event.
A8N5E6
D2CSU5
CM2_PETHY
Chorismate mutase 2
Petunia
MACGDYDDKLSLDLIRDSLIRQEDTIIFNLIERIKFPINSTLYKKPSSWFPDFTGSLFQYLFQETEALQSKVGRYLSPEENPFFPDNLPASIVPPSKCPPVLHPVAESININEKILDVYLNQLLPLFCTEADEGNYATTAACDIQLLQAISRRIHYGKFVAEVKFRDCSDEYTPLILAQQDRDALMKLLTFEVVEEMVKKRVAKKAMIFGQEVTLVDNAKEVKCKVDPLLVSRLYDEWIMPLTKHVQVEYLLRRLDQNKLTSI
Mediates the conversion of chorismate to prephenate.
D2CSU5
Q5MZV1
NADK1_SYNP6
ATP-dependent NAD kinase 1
Synechococcus
MQLRQVIIAYKAGDPTSKAAADDCAHCLESQGIHVMLGPSGARDNPFPVFLASATEPIDLAIVLGGDGTVLAAARHLSDAGIPLLTFNVGGHLGFLTQPRDFFQPEAELWDRLRNDQYAVEQRMMLAASLHEGGRENREPISETYYALNDMCVKPAAPDRMSVCILEMEVDGEIIDQYQGDGLIVSTPTGSTCYTAAAHGPIVHPGVDALAVTPICAMSLSSRPIVIPPRSVVSVWPLGTQDPTIKLWMDGVLATSIWPGQRVDIRMAEKPAQFLVLDSDRSFYRILREKLQWAGAVIHYNNNFRN
Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Q5MZV1
Q8TCB7
METL6_HUMAN
Methyltransferase-like protein 6
Homo
MASLQRKGLQARILTSEEEEKLKRDQTLVSDFKQQKLEQEAQKNWDLFYKRNSTNFFKDRHWTTREFEELRSCREFEDQKLTMLEAGCGVGNCLFPLLEEDPNIFAYACDFSPRAIEYVKQNPLYDTERCKVFQCDLTKDDLLDHVPPESVDVVMLIFVLSAVHPDKMHLVLQNIYKVLKPGKSVLFRDYGLYDHAMLRFKASSKLGENFYVRQDGTRSYFFTDDFLAQLFMDTGYEEVVNEYVFRETVNKKEGLCVPRVFLQSKFLKPPKNPSPVVLGLDPKS
S-adenosyl-L-methionine-dependent methyltransferase that mediates N(3)-methylcytidine modification of residue 32 of the tRNA anticodon loop of tRNA(Ser), including tRNA(Ser)(UGA) and tRNA(Ser)(GCU) . Interaction with SARS1/SerRS is required for N(3)-methylcytidine methylation .
Q8TCB7
A5GP57
HRCA_SYNPW
Heat-inducible transcription repressor HrcA
unclassified Synechococcus
MELLPRRQQEVLQATVHHYVDTIEPVGSKTLVQRFGLQASSATVRSAMGALEQKGLLVQPHPSAGRIPSPRGYRHYVDCLLPKPGAAVHHLEQELTQLSLRWAALDDLLQQLTRRLTDFTGLMSLITLPQPSEQRLHAIRLVPTDERLLVMLVADSSQTHHLNLRLPHGSVHQVAALERWTDDQLHQSGQISWESLPQQLQTCGQALREALHNEEGRFISPSDQSAHVHGVSRLVAQPEFSDSTKVAPLLDLMDCNPAAFIPSGPGHDDWVWIGGEHPHTALSDCSVIQSSYRDGQGGVGQVALVGPMRMAYATARAAVQCVAKHLNHLLS
Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons.
A5GP57
Q02EZ4
SELO_PSEAB
Protein adenylyltransferase SelO
Pseudomonas
MKSLDDLDFDNRFARLGDAFSTEVLPDPIAEPRLVVASPAALALLDLPAETSDEALFAELFGGHKLWSEAEPRAMVYSGHQFGSYNPRLGDGRGLLLGEVINQAGEHWDLHLKGAGQTPYSRMGDGRAVLRSSIREFLASEALPALGIPSSRALCVIGSSTPVWREKKESAATLLRLAPSHVRFGHFEYFYYTRQHDQLKQLAAFVQEHHFADCNAAERPYAAMFRQVVERNAELIARWQAYGFCHGVMNTDNMSILGITFDYGPYAFLDDFDANHICNHSDDAGRYSFSNQVPIAHWNLAALAQALTPLVEVDELRASLDLFLPLYQAHYLDLMRRRLGLGVAAENDQALVQELLQRMQGSAVDYSLFFRRLGEETPERALASLRDDFVDREAFDRWAEAYRRRVEEEGGDQESRRRRMHAVNPLYVLRNYLAQQAIEAAEQGDYTEVRLLHQVLSRPFEEQPGMERFTRRPPDWGRHLEISCSS
Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
Q02EZ4
A2BQS1
ACCD_PROMS
Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
Prochlorococcus
MSLIDWFAARRKDQFVGKVSQDTDEGDGLWVKCSECSQVAYRKDLISNFNVCNNCGHHNRINSDERINIIADKNSFKEFDSLLSPTDPLGFKDRRAYADRIKESQAGTGLRDGVVTGICSVNSMPLALAVMDFRFMGGSMGSVVGEKITRIIERATLENFPILIVCASGGARMQEGMLSLMQMAKISGALKKHKEKNLLYMPLLTHPTTGGVTASFAMLGDLILAEPKALIGFAGRRVIEQTLREKLPDNFQTAEYLLEHGFVDVIVKRKDLKDTLTKILKIHGVKELAEANT
Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
A2BQS1
Q6HC26
MEND_BACHK
Menaquinone biosynthesis protein MenD
Bacillus cereus group
MNNHIEALSYYLGAFVDELTRLNVCDVVISPGSRSTPIALLMEQHEGMNTYLHVDERSAGFFALGIAKAKKRPVALLCTSGTAAANYYPAVCEAFHSRVPLIVLTADRPHELRDVGAPQAMNQINLYGTFVKQFTEMALPEASEAMYHYARMTTQRMIASACLAPQGPVHLNFPVREPLIPDFSLESLWDKGRGEYTGVVQQGNAVMPSEYVDSLVGRLSHMKKGLIICGDDSHSEIATFATQLAEKTGYPILADPLSNIRSGHHDKTMVIDCYDTFLRNELLKETWKPDVLIRFGGMPVSKALTQFIKKQTKAVHIVVDESGQWRDPALVATEVVQASDIAFCSALIEKMPVMKKNDWFRMWQHINEKTKETLREMETYDTAFEGRVITDIVRVLPEGATLFASNSMPIRDTDSFFFTSDKTIQVMANRGVNGIDGIISTALGASMICDPLVLVIGDLSFYHDLNGLLAAKLHELNITIVVVNNDGGGIFSFLPQYEKKEHFESLFGTPIGLDYEHVVTMYGGSFSRVNGWEQFREEVQKGATTEGLHVVEICTNRDENVTLHRKLWAKTQDVITTSLQGESK
Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
Q6HC26
P0C0M3
GH311_ORYSJ
Auxin-responsive GH3-like protein 11
Oryza sativa
MDDHNLDYKGSGALEELEMLTVNAKEAQELILTKILERNQATEYLSKFMNGSTNISAFKRHVPVVTYDKVHPYILRIATGEESSILCGEYILELLRSSGTSRGEPRLMPSILKDLDRRTYLYSLIMPIMNKYISGLGEGKAMYLLFVKAETLTDSGIPVRSVLTSYYKSPHFLHRKHDLYNNYTSPDEVILCPDSQQSMYCQLLCGLVERQHVLRIGAVFASAFLRSISFLEQHWRDLVNDIRIGQLNSSITSPACRLAMLNFLALPNPELADQVEAICSCGSWKGILGRLWPNVKYIEAVLTGTMAQYIPMLEFYGGGAIPFVCTMYASSESYFGVNLSPLCSPADVSYTILPNMAYFEFIPLEDGLRLTDHEEVIENDKLVSLVDVKVGCYYELVVTTFSGLYRYRVGDVLQVTGFYNRAPQFKFICRRNVILSIDSDKTNEEDLHNSVTTAKKILENQNYLLLEYTSYTDISTVPGHYVLFWEIKSTHDERPAPLDAQLLESCCAAVEESLDYVYRRCRAHDRSIGPLEIRLVEAGAFDALMDLLVSHGSSINQYKTPRCIESSLALKLLNSKVIACFFSPQDPECGM
May catalyze the synthesis of indole-3-acetic acid (IAA)-amino acid conjugates, providing a mechanism for the plant to cope with the presence of excess auxin.
P0C0M3
Q5R8C4
EIF3M_PONAB
Eukaryotic translation initiation factor 3 subunit M
Pongo
MSVPAFIDISEEDQAAELRAYLKSKGAEISEENSEGGLHIDLAQIIEACDVCLKEDDKDVESVMNSVVSLLLILEPDKQEALIESLCEKLVKFREGERPSLRLQLLSNLFHGMDKNTPVRYTVYCSLIKVAASCGAIQYIPTELDQVRKWISDWNLTTEKKHTLLRLLYEALVDCKKSDAASKVMVELLGSYTEDNASQARVDAHRCIVRALKDPNAFLFDHLLTLKPVKFLEGELIHDLLTIFVSAKLASYVKFYQNNKDFIDSLGLLHEQNMAKMRLLTFMGMAVENKEISFDTMQQELQIGADDVEAFVIDAVRTKMVYCKIDQTQRKVVVSHSTHRTFGKQQWQQLYDTLNAWKQNLNKVKNSLLSLSDT
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression.
Q5R8C4
A4J903
Y3054_DESRM
Nucleotide-binding protein Dred_3054
Desulforamulus
MSDSEGGVEVSSPRLLIVTGMSGAGKTQAVQSLEDLGYFCVDNLPPALIPKFAELVSQSNGKVEKVALVVDIRGGAFFHQAIEVLHDLGEQGYRFEVLFLEASDETLVRRYKESRRRHPLDNHGEVLKVIQEERELLREIRGRATKVIDTSNVSNNQLKEQIITQYGGDKENSNRLLITVISFGYKYGIPMDSDLVLDVRFLPNPYYIPELRCLTGNDEPVQQHVMSQDVTKEFMEKLIDFVQFLVPHYQREGKATLMIAIGCTGGMHRSVTLTNKLGEVLSEKGYRVNVRHRDIMRV
Displays ATPase and GTPase activities.
A4J903
B4U045
SYY_STREM
Tyrosyl-tRNA synthetase
Streptococcus
MNIFEELKARGLVFQTTDEEALVKALTEGQVSYYTGYDPTADSLHLGHLVAILTSRRLQLAGHKPYALVGGATGLIGDPSFKDAERILQTKETVLDWSQKIKEQLSCFLDFDNGENKAELVNNYDWFSQISFIDFLRDVGKHFTVNYMMSKDSVKKRIETGISYTEFAYQVMQGYDFYELNAKHNVTLQIGGSDQWGNMTAGTELLRKKADKTGHVMTVPLITDATGKKFGKSEGNAIWLDAKKTSPYEMYQFWLNVMDDDAVRFLKIFTFLSLDEIAAIEEQFNAARHERLAQKTLAREVVTLVHGEAAYQQALNITEQLFAGAIKNLSAAELKQGLSNVPNYQVQAEDSLNIVDMLVTAGISPSKRQAREDLQNGAIYLNGERLQDLDYSLSTADRIDNQLTVIRRGKKKYAVLTY
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
B4U045
Q874M2
NBP35_CANGA
Nucleotide-binding protein 35
Nakaseomyces/Candida clade
MSTEVISTSVVSEPTQEILPAEYSLDAPEPEHCPGPESEMAGKADACQTCENKDICESLPKGPDPDIPLITENLSGIKHKILVLSGKGGVGKSTFTTMLSWALSADDNLQVGAMDLDICGPSLPHMLGCTDEVVHESNTGWTPVYVAENLAAMSIQFMLPEDDSAVIWRGNKKNLLIKKFLKDVVWDDLDYLVVDTPPGTSDEHISINKYMKESGIDGALVVTTPQEVALLDVRKEIDFCRKAGINILGLVENMSGFVCPNCKGESQIFKPTTGGGEALCKELGIKFLGSVPLDPRIGRCSDEGESFLDEFPDSPATLAVLNVVEELRDAVGDV
Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NBP35-CFD1 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. Required for biogenesis and export of both ribosomal subunits, which may reflect a role in assembly of the Fe/S clusters in RLI1, a protein which performs rRNA processing and ribosome export.
Q874M2
Q38WF1
G6PI_LATSS
Phosphohexose isomerase
Latilactobacillus
MAHISFDASRLDKFVQSNELAEMQAMVNAADSQLREGTGAGNDFRGFLDLPVNYDKDEFARIKEAVAKIKSDSEIFVAIGIGGSYLGAKAAIDFLNNTFYNMLPAEQRDFPQVLFAGNSISSSYLSDLVNLIGDRDFSINVISKSGTTTEPSIAFRVLKDKLIKKYGKEEAKGRIYATTDRAKGALKTESDAEGYAEFVVPDDIGGRFSVLTAVGLLPIAVAGGDIDQLMKGAADARLEYTDTDVTKNDAYKYAALRNILYRKGYTTELLENYEPTLQYFSEWWKQLMGESEGKDQKGIYPSSANFSTDLHSLGQYIQEGRRNLMETVVNVEKPNSDIDIPADEQNLDGLGYLEGHTMDFVNKKAYQGVVLAHTDGGVPVMTVNIPDQTAYTLGYMIYFFEMAVSISGYLNGINPFNQPGVEAYKKNMFALLGKPGFEELGKELNERL
Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Q38WF1
Q2KZE4
KAD_BORA1
Adenylate monophosphate kinase
Bordetella
MRLILLGPPGAGKGTQATFITQTYGIPQISTGDMLRAAVKAGTPLGIEAKKVMDAGGLMPDEIIIGLVKDRLAQPDCANGYLFDGYPRTIPQADALKDAGVKLDYVIEIAVPDEDIVKRMSGRWVHLASGRSYNTQSNPPKVAGQDDITGEALIQRDDDREETVRHRLGIYQQQTRPLVDYYSSWAAQDPANAPKYRKISGVGSVEEIKARAAAALQS
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Q2KZE4
A0QSE0
RS17_MYCS2
30S ribosomal protein S17
Mycolicibacterium
MADQKGPKYTPAAEKPRGRRKTAIGYVVSDKMQKTIVVELEDRKSHPLYGKIIRTTKKVKAHDENGEAGIGDRVSLMETRPLSATKRWRLVEILEKAK
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
A0QSE0
P0A1K2
FLIJ_SALTI
Flagellar FliJ protein
Salmonella
MAQHGALETLKDLAEKEVDDAARLLGEMRRGCQQAEEQLKMLIDYQNEYRSNLNTDMGNGIASNRWINYQQFIQTLEKAIEQHRLQLTQWTQKVDLALKSWREKKQRLQAWQTLQDRQTAAALLAENRMDQKKMDEFAQRAAMRKPE
Flagellar protein that affects chemotactic events.
P0A1K2
Q96RD9
FCRL5_HUMAN
Immune receptor translocation-associated protein 2
Homo
MLLWVILLVLAPVSGQFARTPRPIIFLQPPWTTVFQGERVTLTCKGFRFYSPQKTKWYHRYLGKEILRETPDNILEVQESGEYRCQAQGSPLSSPVHLDFSSASLILQAPLSVFEGDSVVLRCRAKAEVTLNNTIYKNDNVLAFLNKRTDFHIPHACLKDNGAYRCTGYKESCCPVSSNTVKIQVQEPFTRPVLRASSFQPISGNPVTLTCETQLSLERSDVPLRFRFFRDDQTLGLGWSLSPNFQITAMWSKDSGFYWCKAATMPYSVISDSPRSWIQVQIPASHPVLTLSPEKALNFEGTKVTLHCETQEDSLRTLYRFYHEGVPLRHKSVRCERGASISFSLTTENSGNYYCTADNGLGAKPSKAVSLSVTVPVSHPVLNLSSPEDLIFEGAKVTLHCEAQRGSLPILYQFHHEGAALERRSANSAGGVAISFSLTAEHSGNYYCTADNGFGPQRSKAVSLSVTVPVSHPVLTLSSAEALTFEGATVTLHCEVQRGSPQILYQFYHEDMPLWSSSTPSVGRVSFSFSLTEGHSGNYYCTADNGFGPQRSEVVSLFVTVPVSRPILTLRVPRAQAVVGDLLELHCEAPRGSPPILYWFYHEDVTLGSSSAPSGGEASFNLSLTAEHSGNYSCEANNGLVAQHSDTISLSVIVPVSRPILTFRAPRAQAVVGDLLELHCEALRGSSPILYWFYHEDVTLGKISAPSGGGASFNLSLTTEHSGIYSCEADNGLEAQRSEMVTLKVAVPVSRPVLTLRAPGTHAAVGDLLELHCEALRGSPLILYRFFHEDVTLGNRSSPSGGASLNLSLTAEHSGNYSCEADNGLGAQRSETVTLYITGLTANRSGPFATGVAGGLLSIAGLAAGALLLYCWLSRKAGRKPASDPARSPSDSDSQEPTYHNVPAWEELQPVYTNANPRGENVVYSEVRIIQEKKKHAVASDPRHLRNKGSPIIYSEVKVASTPVSGSLFLASSAPHR
May be involved in B-cell development and differentiation in peripheral lymphoid organs and may be useful markers of B-cell stages. May have an immunoregulatory role in marginal zone B-cells.
Q96RD9
B9KHC9
DAPE_ANAMF
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase
Anaplasma
MRLDDPVSLACRLMSYPSVTPDRSGAIPFLAELLSDLGFRCEILSFGNGDVEVKNLYAQYGNGHPNLCFAGHTDVVPPGGTWRTDPFSPQVKDGMLYGRGASDMKAAICAYISAVARLDSVPGCLSFLITGDEEGRWREYGTKSVLDWMTKNGICPDYCVLGEPSSRKRLGDCISIGRRGSLNFELSCRGVQGHVAYPELAHNPIDDVLCILRKIKDTTLDSGTDHFPPSHCEITSIDVGNDVENLIPSSATAAFNIRFNDLHTAESLYRDMDAICASVTSNYTLSHRCFGGASISQPSCYTATLCEVVKEVTGLDARLITDGGTSDACIISSFCPVAELGLPSGTAHKVDECVSVADVLTLAEIYHRFINRFFAVAQSRS
Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls.
B9KHC9
Q4UU97
CHEB2_XANC8
Protein-glutamate methylesterase/protein-glutamine glutaminase 2
Xanthomonas
MTLETPVRVLIVDDSAVVRQMLTEILSRDPGIEVVGSAADPLLAREKIKRLNPDVITLDVEMPRMDGLVFLENLMRLRPTPVVMISSLTERGADTTLQALSLGAVDFISKPKIDVARGLEGYAEEIVSKVKMAAKAKVSALNRPSAPKITLDMQSAPVPGSALRFRTTDRLIAIGASAGGTEALRVVLEHMPADAPAVVMTQHLPASFSTAFAERLNRHSAMSVREASDGEAILPGHAYLPPGGQHLRIIRDGARWRCRIDDGPPVNRHKPAVDVLFRSVAANAGPNAVGAILTGMGDDGARGLLEMLQAGAPTLVQDEASSVVWGMPGAAYKLGAAQEVVPLERVAERLIALSAQAR
Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.
Q4UU97
E1ZZF9
FMRF_CAMFO
GKNDLNFIRF-amide
Camponotus
MLVSSSVLKDDSSLRIFKESPNEFEYIIKRHDMDDRKEDTESKERRSTMGSSFIRFGRGQSFFNNLDNSAFDNEIDSKVSRHPRWKSPDIVIRFGRSGMKSTNDEQPKRGKNDLNFIRFGRNIQIVPTDFDLSAVCSALMSNDAISDAGLHPDVTRLFRLCNNLNKITGEISLDSLETNSNHRE
In insects, FMRFamide and related peptides have modulatory actions at skeletal neuromuscular junctions, and peptides that are immunologically related to FMRFamide are released into the circulation from neurohemal organs.
E1ZZF9
P81198
H34_STYLE
Histone H3-4
Stylonychia
QTGAKAPRKALANKAARKTAPADGGVKKPHRFRPGTVALREIRKYQKSTELLIRKLPFQRLVREIASDYKSDLRFQSSAVAAIQEAAEAYMVGLFEDTNLCAIHAGRVTIMP
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
P81198
Q5WG44
QUEF_ALKCK
PreQ(0) reductase
Alkalihalobacillus
MAGRQEKELQNVTLLGSEQTEYKYSYDPRVLETFDNQHPYRDYMVKFNCPEFTTLCPKTGQPDFATLYISYIPEQKMVESKSLKLYLFSFRNHGDFHEDSVNTIMNDLIELMDPRYIEVWGKFTPRGGISIDPYCNYGKKGTKYEEIANYRLMNHDLYPETITNR
Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
Q5WG44
Q9R1B1
T10B_RAT
TIMM10B
Rattus
MEHQQQQLRNLRDFLLVYNRMTELCFQRCVPSLHHRALDAEEEACLHSCAGKLIHSNHRLMAAYVHLMPALVQRRMADYEAASAVPGVPAEQPRDSPSGS
Component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. The TIM22 complex forms a twin-pore translocase that uses the membrane potential as the external driving force. In the TIM22 complex, it may act as a docking point for the soluble 70 kDa complex that guides the target proteins in transit through the aqueous mitochondrial intermembrane space.
Q9R1B1
A1TZG0
PYRD_MARN8
Dihydroorotate oxidase
Marinobacter
MYGLLRNLLFRLPPERAHNVALGSLDVAQKLGILNTFTRQPEPCPVNVMGLEFPNPVGLAAGLDKNADHIDALGALGFGFIEVGTVTPLAQPGNPKPRMFRLPEHQAIINRMGFNNEGLEHLITNVRHRRYRGVLGINVGKNKDTPNEQSEQDYRKGIAAVYPYADYITVNVSSPNTPGLRDLQFGDSLKQLLHAIKEEQAACEQKHGRYVPVAVKIAPDMDEQGIRFVAAALLEAGLDGVIATNTTISREAVKGHVHEQEAGGLSGAPVREASVKVIQGLYAELGDRLPIIGVGGITDGDSAAEKIRAGAKLVQIYTGFIYRGPSLINEAVEAIRKEIS
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
A1TZG0
P36907
CHIX_PEA
Endochitinase
Pisum
MKRTLKVSFFILCLLPLFLGSKAEQCGSQAGGAVCPNGLCCSKFGFCGSTDPYCGDGCQSQCKSSPTPTIPTPSTGGGDVGRLVPSSLFDQMLKYRNDGRCAGHGFYTYDAFIAAARSFNGFGTTGDDNTKKKELAAFLAQTSHETTGGWPTAPDGPYAWGYCFVSEQNTQEVYCSPKDWPCAPGKKYYGRGPIQLTHNYNYGLAGQAIKEDLINNPDLLSTNPTVSFKTAIWFWMTPQANKPSSHDVITGRWTPSAADSSAGRVPGYGVITNIINGGIECGHGQDNRVDDRVGFYKRYCQIFGVDPGGNLDCNNQRSFA
Defense against chitin-containing fungal pathogens.
P36907
Q28NZ8
CCMA_JANSC
Heme exporter protein A
unclassified Jannaschia
MVLTVTDLACARGPAQVLSGVSFSVSAGEALILRGPNGAGKTTLLRTLAGLTPPLAGTISHAEDAIAYAAHADGLKAQLTVAENLTFWATIFGTLDIAPAIAAFALAPLADRPAGELSAGQKRRLSLARLLVTGRPIWALDEPTVSLDTENTARFAAAVEAHLRAGGAAIIATHIDLGLPNARSLDITPFIAKGLPASDPFADDPFLGAAL
Part of the ABC transporter complex CcmAB involved in the biogenesis of c-type cytochromes; once thought to export heme, this seems not to be the case, but its exact role is uncertain. Responsible for energy coupling to the transport system.
Q28NZ8
Q9RTQ2
ARGJ_DEIRA
Arginine biosynthesis bifunctional protein ArgJ beta chain
Deinococcus
MTEPLPDVTFPQGFRAAAMAAGIKPSGKPDLSCVVSERDCAWAFAGTRSTTAAACVTRNRELYASGAPLRALVVNAGVANAATGQQGARDNADMADALASVLAVGEAEVITASTGVIGHLLPMDKVLSGVEHLPEELEGAALPFATAIMTTDTRSKLAHVTLSNGARIVGTAKGSGMIHPDMATMFAFAFTDAQVDQGALRGAFPAIVARTFNAVTVDGDTSTNDMTAVLANGAAGETDLTEFLTALEGVMRDLARQIAADGEGATRLLTVRVTGAASEAEALGAARTCCVSPLLKSAVHGADPNWGRVIMAVGRSGAGVKVEAMKVSVQGVPVFAGGPLNYDAAAVSQSMKTDEVIFDVDLGVGSARGEAWGCDLSAEYVSINADYTT
Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.
Q9RTQ2
A3N6H4
KYNB_BURP6
N-formylkynurenine formamidase
pseudomallei group
MDTIWDISPPIAPATPVWPGDTPVGIERVWRIEAGSPVNVARVTLSPHTGAHADAPLHYDADGAPIGAVPLDAYLGRCRVIHCIGARSAVTPGHVRAALDGAPPRVLLRTYGQAPQHAWDSAFCAVAPETIDLLAAHGVRLVGIDTPSLDPQESKTMDAHRRIRAHRMAILEGLVLDEIAAGDYELIALPLKFATLDASPVRAVLRALPAAPR
Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation.
A3N6H4
A5W7Q4
COBT_PSEP1
N(1)-alpha-phosphoribosyltransferase
Pseudomonas
MTQAWWRDACQPLDNAAMDQARARQQQLTKPAGSLGQLEALAIQLAGLQGLERPTLDQVAITIFAGDHGVVEEGISAYPQAVTGQMLCNFVGGGAAISVLARQLQASLDVVDLGTIDAQLELPGVRHLRLGTGTANFARQPAMTENQLQAALQAGRDSAQRGAEQGAQLFIGGEMGIGNTTAAAALASVLLGCPASELSGPGTGLDNAGVQHKAEVIERALRLHGLRAEDPLQVLGCVGGFEIAALVGAYIGCAQAGVAVLVDGFICSVAALVAVRLNPQCRAWLLFAHQGAEPGHKTLLAALQAEPLLALGLRLGEGSGAALAVPLLRLACALHGQMATFAEAAVADRPA
Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
A5W7Q4
G8QM61
SIGF_AZOOP
ECF RNA polymerase sigma factor SigF
Azospira
MQRINREESFRAKEERLKDLFVRGLSGNNAAYQTFLGELSSYLRAFLRKRLIRLPDEVEDLVQEALLAVHNQRHTYDPSQPLSAWVQAIARYKLVDLFRRRAIYEQRNDTLDDGMDLFSSADAEAAEARRDLNKLLADLPDHFRLPIMHTKLEGLSVREAADVSGMSESAIKVGVHRGLKALAAKIRGAL
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma factors are held in an inactive form by a cognate anti-sigma factor (NrsF in this case) until they are released (Probable). Regulates expression of only a few genes (Dsui_0154 to Dsui_0159) in response to (hypo)chlorite, conferring resistance to reactive chlorine species (RCS) during oxic growth .
G8QM61
A6TWL0
ISPD_ALKMQ
MEP cytidylyltransferase
Alkaliphilus
MAVASKVTVIVVAAGKGKRMGRSYNKQYIMLENKPILYHTLAVFEKHSEINEIILVVASGEEEYCQGQIIKKYGLKKVRKVVAGGSERRNSVKNGLEELEEACEVVLVHDGARPFITKEVITKSIEVAYEEGAVIVAVPVKDTIKRVNEKMEVVETPERQQLWAVQTPQVFRSGILKRAYKEAEDFERVGTDDAVLVEAAGYTVKVVLGIYENIKVTTPEDLIIGQGILNQRKDGEQCEWE
Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
A6TWL0
B3PPF1
AROB_RHIE6
3-dehydroquinate synthase
Rhizobium
MNAITSAPAAQTVHVPLGERAYDILIGPGLIARAGAEIASRLKGRKAAIITDENVAPLYLDALVASLDAAGIASAAVVLPAGEKTKSFEHLMTACDKVLEARVERNGCVIALGGGVIGDLSGFAAGIVRRGVRFVQVPTSLLAQVDSSVGGKTGINSRHGKNLIGVFHQPDLVLADTDVLNSLSEREFRAGYAEVAKYGLIDKPDFFAWLEANWKAVFTGGAARIEAIATSCQAKADVVVADERENGQRALLNLGHTFGHALEAATAYDSRRLVHGEGVSIGMVLAHEFSARMNLASPDDARRVERHLQAVGLPTRMAEIPGELPPAEVLMDAIAQDKKVKGGKLTFILTRGIGQSFVADDVPASEVISFLREKHP
Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
B3PPF1
B7VJT5
RLMN_VIBA3
tRNA m2A37 methyltransferase
Vibrio
MTTAKVNLLDFDRKGLRKFFTEELNEKAFRAEQVMKWIYHFGVDDFEQMNNINKKLREKLLHRCEIVAPIVSEAQHSADGTIKWAMSVGDQDVETVYIPDGDRATLCVSSQVGCALECKFCSTAQQGFNRNLKVSEIVGQIWRAAREIGLEKETGRRPITNVVMMGMGEPLLNMKNLIPSLELMLDDLGFSLSKRRVTVSTSGVVSGLDQMTDNIDVALAISLHAPNDALRSQIMPINDRWDIQDFLASVRRYIASSNANRGKVTVEYVLLDHVNDDMDHARELAELMKDTPCKINLIPFNPYPGSPYKKPSNSRIDRFQKTLMEYNYTVTVRKTRGDDIDAACGQLVGDVIDRTKRTKMLKAASEANLIAGDVIQVKAV
Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity.
B7VJT5
Q6Z4U4
BAK1_ORYSJ
Somatic embryogenesis receptor kinase 1
Oryza sativa
MAAHRWAVWAVLLLRLLVPAARVLANMEGDALHSLRTNLVDPNNVLQSWDPTLVNPCTWFHVTCNNDNSVIRVDLGNAALSGTLVPQLGQLKNLQYLELYSNNISGTIPSELGNLTNLVSLDLYLNNFTGPIPDSLGNLLKLRFLRLNNNSLSGSIPKSLTAITALQVLDLSNNNLSGEVPSTGSFSLFTPISFANNPSLCGPGTTKPCPGAPPFSPPPPYNPPTPVQSPGSSSSTGAIAGGVAAGAALLFAIPAIGFAWYRRRKPQEHFFDVPAEEDPEVHLGQLKRFSLRELQVATDTFSNKNILGRGGFGKVYKGRLADGSLVAVKRLKEERTPGGELQFQTEVEMISMAVHRNLLRLRGFCMTPTERLLVYPYMANGSVASRLRERPPSEPPLDWRTRRRIALGSARGLSYLHDHCDPKIIHRDVKAANILLDEDFEAVVGDFGLAKLMDYKDTHVTTAVRGTIGHIAPEYLSTGKSSEKTDVFGYGIMLLELITGQRAFDLARLANDDDVMLLDWVKGLLKEKRLEMLVDPDLQSNYIDVEVESLIQVALLCTQGSPTERPKMAEVVRMLEGDGLAERWEEWQKIEVVRQEVELGPHRNSEWIVDSTDNLHAVELSGPR
LRR receptor kinase involved in defense response . Does not seem to be required specifically for XA21-mediated immunity or basal resistance to Xanthomonas oryzae pv. oryzae (Xoo), or immunity to Magnaporthe oryzae . Involved in brassinosteroid (BR) signaling pathway. Acts as coreceptor of BRI1. Forms at the plasma membrane a receptor complex with BRI1 which is activated in response to brassinolide. Phosphorylates BRI1 . Required for normal plant growth and leaf development . Possesses kinase activity in vitro .
Q6Z4U4
Q7YR25
ABC3G_CHLAE
Deoxycytidine deaminase
Chlorocebus
MNPQIRNMVEQMEPDIFVYYFNNRPILSGRNTVWLCYEVKTKDPSGPPLDANIFQGKLYPEAKDHPEMKFLHWFRKWRQLHRDQEYEVTWYVSWSPCTRCANSVATFLAEDPKVTLTIFVARLYYFWKPDYQQALRILCQERGGPHATMKIMNYNEFQHCWNEFVDGQGKPFKPRKNLPKHYTLLHATLGELLRHVMDPGTFTSNFNNKPWVSGQRETYLCYKVERSHNDTWVLLNQHRGFLRNQAPDRHGFPKGRHAELCFLDLIPFWKLDDQQYRVTCFTSWSPCFSCAQKMAKFISNNKHVSLCIFAARIYDDQGRCQEGLRTLHRDGAKIAVMNYSEFEYCWDTFVDRQGRPFQPWDGLDEHSQALSGRLRAI
DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Exhibits antiviral activity against vif-deficient: HIV-1 and simian immunodeficiency viruses (SIVs) and also simian foamy virus (SFV). After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA. May inhibit the mobility of LTR retrotransposons.
Q7YR25
Q38868
CDPK9_ARATH
Calmodulin-domain protein kinase CDPK isoform 9
Arabidopsis
MGNCFAKNHGLMKPQQNGNTTRSVEVGVTNQDPPSYTPQARTTQQPEKPGSVNSQPPPWRAAAAAPGLSPKTTTKSNSILENAFEDVKLFYTLGKELGRGQFGVTYLCTENSTGKKYACKSISKKKLVTKADKDDMRREIQIMQHLSGQPNIVEFKGAYEDEKAVNLVMELCAGGELFDRIIAKGHYTERAAASVCRQIVNVVKICHFMGVLHRDLKPENFLLSSKDEKALIKATDFGLSVFIEEGKVYRDIVGSAYYVAPEVLRRRYGKEVDIWSAGIILYILLSGVPPFWAETEKGIFDAILEGHIDFESQPWPSISSSAKDLVRRMLTADPKRRISAADVLQHPWLREGGEASDKPIDSAVLSRMKQFRAMNKLKKLALKVIAENIDTEEIQGLKAMFANIDTDNSGTITYEELKEGLAKLGSKLTEAEVKQLMDAADVDGNGSIDYIEFITATMHRHRLESNENLYKAFQHFDKDSSGYITIDELESALKEYGMGDDATIKEVLSDVDSDNDGRINYEEFCAMMRSGNPQQQQPRLF
May play a role in signal transduction pathways that involve calcium as a second messenger.
Q38868
A9B543
HEM1_HERA2
Glutamyl-tRNA reductase
Herpetosiphon
MQLVVVGAHQRTAPISIRERIAFAEAELAQALSSLRQIAVEGFILSTCNRVELYALVEEADGGRSLRQFLAQQRSIDLDELMPHVYTYLDEDAVRHLFRVASGLDSMALGEAQILSQIKTAYNAAQQTELLGTTMHRLIQAALTTGKLVRTETQLAHAQLSVVSVGLSLARQHLDLTNRSVVIIGAGRTGELALKHYLEYTSNITVLSRTFERAARLAEHHKVAAKPISELAAVLQASDVVISCTSSPELMLDFEQAQLLQAQRQRQWVLLDLAVPRDIDRHVGALPEVWLYDVDDMQAICERNRASKAAEVAGAEAIVERELIKWQEWWLTQAVLPTIRALRAHAEAIRLAELERTLARLDLSEQQQQAVSALTSAIINKLLHQPMRAIKDTAASPQLAHAAQQLFRLDFEAI
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
A9B543
Q0T1D5
NORV_SHIF8
Anaerobic nitric oxide reductase flavorubredoxin
Shigella
MSIVVKNNIHWVGQRDWEVRDFHGTEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRNEIDLADIDYIVINHAEEDHAGALTELMAQIPDTPIYCTANAIDSINGHHHHPEWNFNVVKTGDTLDIGNGKQLIFVETPMLHWPDSMMTYLTGDAVLFSNDAFGQHYCDEHLFNDEVDQTELFEQCQRYYANILTPFSRLVTPKITEILGFNLPVDMIATSHGVVWRDNPTQIVELYLKWAADYQEDRITIFYDTMSNNTRMMADAIAQGIAETDPRVAVKIFNVARSDKNEILTNVFRSKGVLVGTSTMNNVMMPKIAGLVEEMTGLRFRNKRASAFGSHGWSGGAMDRLSTRLQDAGFEMSLSLKAKWRPDQDALELCREHGREIARQWALAPLPQSTVNTVVKEETSATTTADLGPRMQCSVCQWIYDPAKGEPMQDVAPGTPWSEVPDNFLCPECSLGKDVFDELASEAK
Anaerobic nitric oxide reductase; uses NADH to detoxify nitric oxide (NO), protecting several 4Fe-4S NO-sensitive enzymes. Has at least 2 reductase partners, only one of which (NorW, flavorubredoxin reductase) has been identified. NO probably binds to the di-iron center; electrons enter from the NorW at rubredoxin and are transferred sequentially to the FMN center and the di-iron center. Also able to function as an aerobic oxygen reductase.
Q0T1D5
Q21L30
RECR_SACD2
Recombination protein RecR
Saccharophagus
MFSPLIDQLINSLRHLPGVGPKSAQRMALHLLERDREGAQNLSEVLAKAVEHVHRCQQCRTLTEQALCNICSNARRNRKELCIVETPADVIAIETSAVFSGYYFVLLGRLSPIDGIGPKEIGMDVLASRFAEGEIEEVIIATNPTIEGEATAHYISERAKAQGIKVSRIAHGIPIGGELEYVDGGTLAHAISRRQEI
May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.
Q21L30
Q2LVU5
RNH2_SYNAS
Ribonuclease HII
Syntrophus
MIGMDHFEREAYEDGYRVIAGVDEAGRGPLAGPVVAAAVILPHGYSHPEITDSKKLSAGKREKLYEVIKRDALAIGVGVVESPVIDQVNILRATLRAMAEAVDDLSIRPDFLLVDGLHRIFLNISQKTIVKGDTLSVSIASASIIAKVSRDRIMEIYHRQFPQYNFLKNKGYGTREHREAIQNFGFCKIHRRSFKVKSTKPQSLQTVNLFDF
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Q2LVU5
P55876
IF5_MAIZE
Eukaryotic translation initiation factor 5
Zea
MALQNIGASNRDDAFYRYKMPRMITKIEGRGNGIKTNVVNMVDIAKALARPASYTTKYFGCELGAQSKFDEKTGISLVNGAHDTAKLAGLLEVFIKKYVQCYGCGNPETEILISKTQMISLKCAACGFVSDVDMRDKLTTFILKNPPEQKKGGKDKKAMRRAEKERLKEGEAADEEQKKLKKDAKKKGSKDSTAKGLKKKATTATGSDEDHSSSPTRSHDGDKAAADDDDDDVQWQTDTSIEAAKQRMQEQLSAATAEMVMLSTEETEKKMKQPTHKDGSTNGSAKEIPNDKPAVTKPSPYEELIGDIKASLGSAPTPSQLKAVLASSTLPPQDVMNAPLEALFGGVGKGFTKEVVKNKKYLAVAVPDEGAQTLLVQAIEAFGGKCNPEALKEVPVVLKALYDGDILDEETIVDWYNDAVAAGKDSQVVKNAKPFVEWLQSAESDEEGDDE
Catalyzes the hydrolysis of GTP bound to the 40S ribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent joining of a 60S ribosomal subunit resulting in the release of eIF-2 and the guanine nucleotide. The subsequent joining of a 60S ribosomal subunit results in the formation of a functional 80S initiation complex (80S.mRNA.Met-tRNA[F]).
P55876
Q9ZFC6
DNAK_METSS
Heat shock protein 70
unclassified Methylovorus
MAKIIGIDLGTTNSCVAVMEGGKPRVIENAEGTRTTPSIVAYQDDGEILAGAPAKRQAVTNPKNTLYAVKRLIGRRFEEKEVQKDIGLMPYTITKADNGDAWVEVRGQKMAPPPNSAEVLRKMKKTAEDYLGEEVTEAVITVPAYFNDSQRQATKDAGRIAGLEVKRIINEPTAAALAFGLDKQEGDRKIAVYDLGGGTFDISIIEIAEIDGEHQFEVLSTNGDTFLGGEDFDNRLIDFLADEFKKEKRLDLRNDLLAKQRLKEAAEKAKIELSSAQQTEVNLPYITADATGPKHLVVKITRTKFESLVEDLIERSIKPCEVALKDAGVKPSDIQDVILVGGQTRMPKVQEKVKEFFGKEPRKDVNPDEAVAVGAAIQGGVLQGDVKDVLLLDVTPLSLGIETLGGVMTKLIKKNTTIPTKASQVFSTAEDNQNAVTIQVLQGEREMAAGNKSLGQFNLSDIPPAPRGMPQIEVTFDIDANAILHVSAKDKATGKENKITIKANSGLSEEEIKRMEEDAAAYADEDRKLRELVDARNSADGMVHSVKKSLSEHGDKLEAGEKEKIEAAIKDVEDAIKGDDKEAIEAKTNALMEASQKLGEKVYAEQQAQQGGAEEAQPQGEKTVDADVVDAEFEEVKDDKK
Acts as a chaperone.
Q9ZFC6
B1VFY4
ATPD_CORU7
F-type ATPase subunit delta
Corynebacterium
MHAASREAFERLIKTLDQGLKESDNAVGNGATTGTELFDVVDVLDQERSLRVAMVDAAATPEQRVELVKTLLSGKVTASTEEIVSAAVSQNWSNSQDFRTGLERLGRRALLRSAEAQGQLERVEEELFSLARILERESELELLLSDRAAAVDDRRDLLAKVLYGKVSSVTEALALQAVGRARKAPVDLLDDLCQEAASLNGYEVARVTSAGPLSEEQKASLSEKLHKIYGRKIAVHTEVDSSLLGGAVVRVGDEVIDGSTAGKLERMRRSLA
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.
B1VFY4
B3QMB2
DNAK_CHLP8
Heat shock protein 70
Chlorobaculum
MGKIIGIDLGTTNSCVAVMQGTQPTVIENSEGYRTTPSMVAFTKTGERLIGQAAKRQAVTNPKNTIFSIKRFMGRKYDEVPNEKKFASYDVVNEGGDARVKIGEKSYSPQEISAMILQKMKQTAEDFLGEKVTEAVITVPAYFNDAQRQATKDAGKIAGLEVKRIINEPTAAALAYGLDKKKENEKVAVFDLGGGTFDISILELGDGVFEVKSTDGDTHLGGDDFDQVIIDYLADEFKKQEGIDLRKDAIALQRLKEAAEKAKIELSSRTDTEINLPFITATQEGPKHLVINLTRAKFEAMSATLFDKVLEPCRRALKNSKLDMKEIDEVVLVGGSSRIPKVQALVKEFFGKEPNKSVNPDEVVAIGAAIQGGVLQGDVTDVLLLDVTPLSLGIETLGGVMTKLIEANSTIPTRKQETFSTAADNQTSVEVHVLQGERPMASDNKTLGRFHLGDIPPAPRGIPQIEVTFDIDANGILNVSAKDKATGKEQSIKIEASGKLTEAEIEKMKEDAKAHADEDQKRKEEIDLKNSADSLIFSTEKQLSELGDKLPADKKAEIESALEKLKEAHKAGSADAIKPAMDELSKVWSEAASNLYQQPGAEAGAAPQPETNGQQESKGGDGAVNAEYEVIDGDDDKK
Acts as a chaperone.
B3QMB2
Q42945
CAMT6_TOBAC
Trans-caffeoyl-CoA 3-O-methyltransferase 6
Nicotiana
MAENGAAQENQVTKHQEVGHKSLLQSDALYQYILETSVYPREPEPMKELRELTAKHPWNLMTTSADEGQFLSMLLKLIIAKNTMEIGVYTGYSLLATALALPDDGKILAMDINKENYELGLPVIQKAGVAHKIDFREGPALPVLDLMIEDKNNHGTYDFIFVDADKDNYINYHKRIIELVKVGGVIGYDNTLWNGSVVAPPDAPMRKYVRYYRDFVLELNKALAADPRIEICMLPVGDGITLCRRIS
Methylates caffeoyl-CoA to feruloyl-CoA and 5-hydroxyferuloyl-CoA to sinapoyl-CoA. Plays a role in the synthesis of feruloylated polysaccharides. Involved in the reinforcement of the plant cell wall. Also involved in the responding to wounding or pathogen challenge by the increased formation of cell wall-bound ferulic acid polymers. Methylates almost exclusively caffeoyl-CoA.
Q42945
B4U4I6
RECU_STREM
Recombination protein U homolog
Streptococcus
MVNYPHNPIRQKVTPLQKQQKHRQVDFANRGMSFEAAINATNAYYLAKGIAVIHKKPTPIQIVKVDYPRRSRAKIVEAYFKQASTTDYSGIYKGHYIDFEAKETRQKTAMPMKNFHAHQIEHMAAVLKQKGICFVLLHFATLKETYYLPAKALIDFYQIDRGNKSMPLDYIRKNGFEVKLGAFPQVPYLDIIEQKFLGGDYN
Endonuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves mobile four-strand junctions by introducing symmetrical nicks in paired strands. Promotes annealing of linear ssDNA with homologous dsDNA. Required for DNA repair, homologous recombination and chromosome segregation.
B4U4I6
B3CQT9
ATP6_ORITI
F-ATPase subunit 6
Orientia
MLANPLSQFLIKPIIPLEALGYNISITNSAVAMIFVSIAASMLLITAFVNSKLVPSRWQAFGEILYESNIKLVHSIIGPQGKKFFPLILTLFLFISLGNILGMVPHAFTFTSHIIVTFSLAMIVFTTTLVYGIYRHKLGFFSLFLPKNIPLWLAPIMVIIELCVFISKPISLSLRLTANMVAGHILLKIIAWSIVSLTWLFKPLPIALVIVLIGFELFISILQAYIFTILSCVYLRDVVNLH
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
B3CQT9
Q7S8M2
SPC24_NEUCR
Kinetochore protein 3
Neurospora
MLLEEDPSTLIAHTTQNFNITPDRHAVSRVAESLSTLQQARDLRLRESETNLKKLARTLNTLQSQHQEVTSSHSSAEHASLISRLDTQKFRVAKNVSDLEMETERLQTQLAELQARLQELELQGVDGGDASAAGGATSTGENNGNGSAGNGGQVRSVEDEVLLRLKVYRSLGIEIEREEQDGGEFTRAVVRNDRRGDVCVVNVDRHRFSRFFYANYFWQTL
Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity.
Q7S8M2
A7H2D2
GUAA_CAMJD
Glutamine amidotransferase
Campylobacter
MKKADILVLDFGSQYTQLIARRLREQGVYAEILPFNVSLADIKAKEPKGIILSGGPASVYATDAYFCDKGIFDLGLPVLGICYGMQLMAHHYKATVAPAGHKEYGKANIEVKKDSALFKNLPKKQTVWMSHSDKVENLSQGFEVLATSENSPFCVFGNEDKKFFALQFHPEVQHSEFGKNILKNFAKYACNCESVWNMGSFAKTQAEKIREEVGNDKVLCAVSGGVDSSVVAALLASAIKEQVIVVFVDNGLLRSGEKEQVEFMFKNTLGIDLISIDASEIFLSRLANVRDPEQKRKIIGNTFIEIFEEEAKKHKDVKYLAQGTLYTDIIESSVVGASKTIKSHHNVGGLPEKINLKLIEPLKEIFKDEVRALGLELGLSKEVVYRHPFPGPGLAIRIMGEVNRPSLELLRKADVILLEELKSTGWYDKTWQAFCVLLNVKSVGVMGDNRTYDNAVCIRVVDASDGMTATFSHLPYEVLENISRRIINEVEGINRVVYDISSKPPATIEWE
Catalyzes the synthesis of GMP from XMP.
A7H2D2
Q5P4Z6
TOLB_AROAE
Tol-Pal system protein TolB
Aromatoleum
MNILLSRFRLLLAAALAALSWGAQAQLSIEITGAGATRFPVAIPLFENEGSLPRGITDVVRADLERSGLFSLVDMGLVTLPATAVPDLAGVRARGADAVLAGSLYPQADGRYDVRFRLFDTQKQTELGGLSLRMTPAQNRATAHRIADFVYEKLTGQPGYFATRIAYVVKSGPRYELQIADADGMNAQTALASREPIISPAWAPDGQRLAYVSFEAKKPVVYVHTLATGQRHVVANFKGSNSAPTWAPDGQRLAVVLTKDGQSQLYVLNADGSGLRRMATSPGIDTEPAWSPDGEWIYFSSDRGGSAQIYRIPASGGSAQRVTFEGNYNVTPRLSPDGRSLAFITRNNGRFQVAVMDLATRQTTILTDSSRDESPSFAPNGRMILYATESGGRGVLAAVSSDGRVKQRLSVQAADVREPSWGPLTR
Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
Q5P4Z6
Q14G52
LPXD2_FRAT1
UDP-3-O-acylglucosamine N-acyltransferase 2
Francisella
MYSLDFLASKLDGEVKGDKNVEIKKIATLSQAGEGDISFCTNPKYLKALSETKASAVLITEEVLEFCNTNAVVLSNPYMALAKVMELFDKSPRPDGKIHSKAVIAASAIIGENVTIGANAVVGENVVIGDNVYIGACATIDNGTKIGNDTLIKSNVSIAHDVVIGTGCIIHQNAVIGCDGFGNARDEDGSWTKIPQLGRVIIEDDVEIGSGTTVDRGAIDDTIIKKGARIDNLVQIAHNVVIGRNTALAGVTAVAGSTTIGDNCLIGGQSAITGHISICDNTIIGGASNIGKSITKPGMYYAAFEAKPRIQWGRFVAKLAKIDTLITKVKQLEEKIK
Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Q14G52
P32254
RASS_DICDI
Ras-like protein rasS
Dictyostelium
MFNFKLVLVGPGGVGKSCLTIQFIAQKFVDEYDPTLEDSYRKQTTVDGEECLLDIYDTAGQEDFSAVRDQYMRTGEGFLCVYSITYLQSFKEIHRLHNHLLKVKDLDSVPFVLVGNKCDLNEYREVSTAEGEELAKKLNCKFLETSAKERINVSESFYELVREVKKARQSNQHSNSQEQNTDQPIKKKKSCNLL
Ras proteins bind GDP/GTP and possess intrinsic GTPase activity.
P32254
Q4A1L5
BECN1_PIG
Beclin-1-C 37 kDa
Sus
MEGSKTSSSTMQVSFVCQRCSQPLKLDTSFKILDRVTIQELTAPLLATAQVKPGETQEEEANPGEEPFIETRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLCEECTDTLLDQLDTQLNVTENECQNYKRCLEILEQMHEDDSEQLRMELRELALEEERLIQELEEVEKNRKIVAENLEKVQAEAERLDQEEAQYQREYSEFKRQQLELDDELKSVENQMRYAQMQLDKLKKTNVFNATFHIWHSGQFGTINNFRLGRLPSVPVEWNEINAAWGQTVLLLHALANKMGLKFQRYRLVPYGNHSYLESLTDKSKELPLYCSGGLRFFWDNKFDHAMVAFLDCVQQFKEEVEKGETRFCLPYRMDVEKGKIEDTGGSGGSYSIKTQFNSEEQWTKALKFMLTNLKWGLAWVSSQFYNK
Beclin-1-C 35 kDa localized to mitochondria can promote apoptosis; it induces the mitochondrial translocation of BAX and the release of proapoptotic factors.
Q4A1L5
Q9M175
PTR39_ARATH
Protein NAXT1-like 2
Arabidopsis
MASLVSGDKEAQISGDPGSKRGGWITFPFMLATLLGLSVTSFGWVMNLIVFLIEEFNIKSIAAAQISNVANGCLSMLPVVAAILADSFFGNIPVIAASSFISLLGIVLLTLIASLDYLRPRPCEAGSVLCTPPSKLHLGILYTALALVTTGAGGTRFTMASAGANQYEKPKEQGSFFNWYFLTLYAGAITGATAIVYIQDNASWKLGFGLCAAANLISFIVFVSGKRYYKHDKPMGSPFTSLIRVVVSATVKRKAVISCNEEDYHHYGLEKEVKTSAAMPSKSFRFLNRAALMTKDDLNQKEGSVNNIWRLCSVQEVEDFKAILRVFPLWLSIIFVSTPMVMQTSLIVLQALVTDRGLGPNFKVPAGSLQVIIIITACIVIIMNNWLVFPMYKKLTHKLLTPLQKVGIGQVLTILSMALSAVVEAKRLKTVENGHPMSVLWLFPPLVIVGIGEAFQFPANIELFYGEFPESLRNTATSLTSVVIGISFYLSTALIDLIQRTTAWLPNDINHGRVDNVYWLLVIGGILNFGYFLVCSWVYKYRNLKDNDQEQDPKDGTM
Transporter involved in a passive nitrate efflux.
Q9M175
A0CRL1
EFTS1_PARTE
Elongation factor Ts, mitochondrial 1
Paramecium
MFRKIYTNISITLIKQLREASGSPINDCKKALESTDGNFEKAIQYLKERGLAQAEKKSGNQTKQGVIVAYTNNKVAALAEINCETDFVARTNEFLEFSTNFIKTVVNQEKDFNSSNIESVLRQSQNQAYFETNIDDKRKQLVGKLQENIVIGNLNAFVATNNSIFGVYQHNCLKSTICGLGGSVVELITEQGLNDVKSQILREGANNLAVTYLGLKPKFLYENEVASDVIDLIRKEVQRDFGSKTPQQQNFIVQGKLQNYYSDNVFEHQEYILNEDEPQTIKQYIKKELEDVIKDKVKIGRCLYLTI
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
A0CRL1
P02081
HBBF_BOVIN
Hemoglobin gamma chain
Bos
MLSAEEKAAVTSLFAKVKVDEVGGEALGRLLVVYPWTQRFFESFGDLSSADAILGNPKVKAHGKKVLDSFCEGLKQLDDLKGAFASLSELHCDKLHVDPENFRLLGNVLVVVLARRFGSEFSPELQASFQKVVTGVANALAHRYH
Involved in oxygen transport from the lung to the various peripheral tissues.
P02081
P30154
2AAB_HUMAN
PP2A subunit A isoform R1-beta
Homo
MAGASELGTGPGAAGGDGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTIYDEDEVLLALAEQLGNFTGLVGGPDFAHCLLPPLENLATVEETVVRDKAVESLRQISQEHTPVALEAYFVPLVKRLASGDWFTSRTSACGLFSVCYPRASNAVKAEIRQQFRSLCSDDTPMVRRAAASKLGEFAKVLELDSVKSEIVPLFTSLASDEQDSVRLLAVEACVSIAQLLSQDDLETLVMPTLRQAAEDKSWRVRYMVADRFSELQKAMGPKITLNDLIPAFQNLLKDCEAEVRAAAAHKVKELGENLPIEDRETIIMNQILPYIKELVSDTNQHVKSALASVIMGLSTILGKENTIEHLLPLFLAQLKDECPDVRLNIISNLDCVNEVIGIRQLSQSLLPAIVELAEDAKWRVRLAIIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATNNLMKLVQKFGTEWAQNTIVPKVLVMANDPNYLHRMTTLFCINALSEACGQEITTKQMLPIVLKMAGDQVANVRFNVAKSLQKIGPILDTNALQGEVKPVLQKLGQDEDMDVKYFAQEAISVLALA
The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit.
P30154
P11893
RK24_PEA
CL24
Pisum
MVAMAMASLQSSMSSLSLSSNSFLGQPLSPITLSPFLQGKPTEKKCLIVMKLKRWERKECKPNSLPVLHKLHVKVGDTVKVISGHEKGQIGEITKIFKHNSSVIVKDINLKTKHVKSNQEGEPGQINKVEAPIHSSNVMLYSKEKDVTSRVGHKVLENGKRVRYLIKTGEIIDSEENWKKLKEANKKTAEVAAT
One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
P11893
Q5FUU9
SYP_GLUOX
Prolyl-tRNA synthetase
Gluconobacter
MRLTKAFQPTLKEVPAEAQIASHRLMLRAGLVRQTASGIYAWLPAGLRVLRNIEQIIREEQDAIGAQEVLMPTLQSAELWRRSGRYDAYGPEMLRIQDRHGRDLLYGPTNEEMITDIFGSSVKSYKELPKALYHIQWKFRDEVRPRFGVMRGREFLMKDAYSFDASYEGAVASYRRMMLSYLRIFQRLGVRAVPMVADTGPIGGDLSHEFLVLAPTGESAVFFDAALEEQDWLSRPVDCDDAESLATFFATVTDHYAATDEKHDEAEWAKVPAERKREGRGIEVGHIFYFGTKYTASMGIEVSGPDGAPFHPHMGSYGVGVSRLVGAIIEASHDDAGIIWPASVAPYRAAILNLRQDDEACDAICDRIYGTDPENLLYDDRSERAGVKFNDADLMGHPWQIIVGPRGAKEGKVELKQRATGERFELSVEDALAKIGAA
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro).
Q5FUU9
Q81TQ3
NADK1_BACAN
ATP-dependent NAD kinase 1
Bacillus cereus group
MKFTIMSKGDQSSDTLASTMKEYLLDFGFIMDEQEPDIVISVGGDGTLLYAFHRYYNRLDETAFVGVHTGHLGFYADWLPTEVEKLVIAIAKTPFQVVEYPLLEVIIRYMNGSKESQYLAMNEATVKSAEGTLVTEVEIRGEYFETFRGDGLCISTPSGSTAYNKALGGAIIHPSIEAIQIAEMASINNRVFRTVGSPLVLPKHHTCVLKPTAGMNLQITVDHLTMVHQDVKSIQYRVANEKVRFVRFRPFPFWKRVRDSFVADK
Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Q81TQ3
Q2JTM7
RUVB1_SYNJA
Holliday junction ATP-dependent DNA helicase RuvB 1
unclassified Synechococcus
MAIISSRDTGQNAEGPKRRQQKSSAWRKEGRELSFAGERGADPSALLQPQAHPGEAQEESLRPRTLAEYIGQTELKEVLSIAIAAARARQEPLDHLLFYGPPGLGKTTVAAVLAAEMGSQFYMTTAPALESPRDIAGYLVRLKRGDVLFIDEIHRLPKVTEELLYPAMEDFRLDITIGKGRSARITSLPLERFTLIGATTRIGALTSPLRDRFGHVQRLRFYEPHELVQIVLRTARLLNVSTDPEGAAEIARRSRGTPRIANRLFKRVRDYAQVRGDGHISQEVAAAALELFQVDPMGLDWIDRKLLTVLVEQFGGGPVGLETMAAVTGEDPQTIEEVYEPYLLQIGYLQRTPRGRVVTPAALRHLGYEAQSPLPLWS
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.
Q2JTM7
P53696
PROF_CANAX
Profilin
Candida
MSWQAYIDNLIANGKVDKAALYSRAGDALWAQSGSFELQQPEITEIAKGFDSAEGLQTSGLHVQGQKYFLLRADDRSIYGKHEAEGVICVRTKQTILIAHYPSGVQPGEATTLVEKLADYLINVGY
Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG.
P53696
P0CN11
DOHH_CRYNB
Deoxyhypusine monooxygenase
Cryptococcus neoformans species complex
MSVQVSPEQMATLKATLLNTPGNVPLHERFRALFMLKAVGGDEVVDIVSEGLKDPSPLLKHELAYVLGQLLNTRALPTLSRVLENPTGEHCSMVRHEAAEALGAIGAEESLPILRKYMQDENREVRETCEIAVGKIEFDLSEEGKKANANPDFPTIDPAPSAAPSDIPSLRADLLNTSLPLFQRYRAMFALRDFGAGSKEAVEALADGFRDGSALFRHEIAYIFGQLSSPYSIPSLLSRLRDAKEDDMVRHEAAEALGGIASDGVESENPEVVLPEDERLPEGGVLAVLREWAVKADAPTVVRESCQVAIDMWEYENSADQFNPLDSLSAKQEEREKTEKVNTTGMERSAHAAVAAMGIAA
Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor.
P0CN11
C4ZQE0
RUTA_ECOBW
Pyrimidine monooxygenase RutA
Escherichia
MQDAAPRLTFTLRDEERLMMKIGVFVPIGNNGWLISTHAPQYMPTFELNKAIVQKAEHYHFDFALSMIKLRGFGGKTEFWDHNLESFTLMAGLAAVTSRIQIYATAATLTLPPAIVARMAATIDSISGGRFGVNLVTGWQKPEYEQMGIWPGDDYFSRRYDYLTEYVQVLRDLWGTGKSDFKGDFFTMNDCRVSPQPSVPMKVICAGQSDAGMAFSARYADFNFCFGKGVNTPTAFAPTAARMKQAAEQTGRDVGSYVLFMVIADETDDAARAKWEHYKAGADEEALSWLTEQSQKDTRSGTDTNVRQMADPTSAVNINMGTLVGSYASVARMLDEVASVPGAEGVLLTFDDFLSGIETFGERIQPLMQCRAHLPALTQEVA
Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism, adding oxygen atoms in the process to yield ureidoacrylate peracid, that immediately reacts with FMN forming ureidoacrylate and FMN-N(5)-oxide. The FMN-N(5)-oxide reacts spontaneously with NADH to produce FMN. Requires the flavin reductase RutF to regenerate FMN in vivo.
C4ZQE0
P0DTH2
APOC4_DICBI
Apolipoprotein C4
Diceros
MSLPGRRPWALPSFCVYVLVLAWVVACQQEVPTGSPSPPPGRASGLWGLVRGKVKEFMEPLVTKTRERWRWFWGPSAFRDFMQTYYDDHLRDLRPRAQAWLRSSKESLLNKAYNMCPQLLCGDGDQG
May participate in lipoprotein metabolism.
P0DTH2
O05505
PTEB_BACSU
Oligo-beta-mannoside-specific phosphotransferase enzyme IIB component
Bacillus
MKKILLACSSGMSTSLLVTKMKEYAQSIGEEAEIWAVGQDKAKEDMRKADAVLIGPQMSFLKSELQKEADQYNIQVEVIDMMAYGMADGKKAYEQALSLMVNQ
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II GmuABC PTS system is involved in the transport of oligo-glucomannans such as cellobiose or mannobiose.
O05505
A3LNF8
KMO_PICST
Kynurenine 3-hydroxylase
Scheffersomyces
MSVLESVDTSNRHQGVGIVGAGLVGCLAALAFAAKGYSVTLFELRPDPKTVDASERNLRSINLAVSNRGIRALKYVDDAMADRILEHIIPMKGRMIHDTTGTKQESQLYGLFGESINSIDRGFLNDCLLAEMRHSDDINVLFNHKLVQLDHLMREDETPTMTFVDTRDNKAEPKTFEFDYIVGADGAHSQFRYQMQRSMRMDFQQKYIDMQYLELYIPPNTLEGATSKFSIDPNHLHIWPRHNFMLIALANKDGSFTSTFFSPWSVIESIKSAQEWVVFFKKNFPDAYKLMGDDHLISVYESNPRGTLMQVTAYPYHNPTGRAIIIGDAAHSMVPFYGQGMNCGFEDVRVLMELIDTNHGNVTKSFKQYSDARKKDLDAICKLALDNYHEMSSKVTSPLYLIRKKLDYTLGKYANGTLFQWLPLYTMISFRDDIPYAKAIAIEKRQATILNRVQIVSLTALALYGAVKAAQCWDRFRR
Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid.
A3LNF8