Datasets:
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Full Name
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147
⌀
taxon
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46
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sequence
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2.75k
function
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5.51k
AlphaFoldDB
stringlengths
6
10
Q604M0
TRUD_METCA
tRNA-uridine isomerase D
Methylococcus
MTGHPDCPGFDDLPRAHGEVTCRGRIRVSPEDFRVDEILGFEPTGQGEHAFLHIRKTGENTDHVAQRIARLAGVKPMDVGYAGLKDRHAVTTQWFSVRLAGKADPDWRALESESIAVLRHTRHDRKLKRGALAGNRFRIILRGLEGVCDGLEARCAAIRAAGVPNYFGPQRFGHGGRNLQEALRLFADPRRRIDRNKRSLYLSAARSYLFNRVLAGRVEHGSWNRGVEGDAFMFTGSNAFFKTDKLDEDIQRRVEALTIHPSGTLWGRGDPVISGTALAMERVALAQCAEFREGLERCGLEVGRRALRLPVPDLEFAGVEDSACELTFSLPAGTYATTVLRELVEFDPQGWPDT
Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
Q604M0
Q6IEY1
OR4F3_HUMAN
Olfactory receptor OR1-1
Homo
MDGENHSVVSEFLFLGLTHSWEIQLLLLVFSSVLYVASITGNILIVFSVTTDPHLHSPMYFLLASLSFIDLGACSVTSPKMIYDLFRKRKVISFGGCIAQIFFIHVVGGVEMVLLIAMAFDRYVALCKPLHYLTIMSPRMCLSFLAVAWTLGVSHSLFQLAFLVNLAFCGPNVLDSFYCDLPRLLRLACTDTYRLQFMVTVNSGFICVGTFFILLISYVFILFTVWKHSSGGSSKALSTLSAHSTVVLLFFGPPMFVYTRPHPNSQMDKFLAIFDAVLTPFLNPVVYTFRNKEMKAAIKRVCKQLVIYKRIS
Odorant receptor.
Q6IEY1
Q0C5X3
TSAD_HYPNA
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
Hyphomonas
MRAMSKSLTILGIETSCDETAAAVLRYEDGRATLLSDVIRTQLAEHAPYLGVVPEIAARAHAELADLTVAAAMNASGLSYAELDGVAATAGPGLIGGVLVGLMTGKAIAQAAGKPFIPVNHLEGHALSPRLSEDCPFPYLLLLVSGGHCQFLDVRGLGDYRRLGSTIDDAVGEAFDKVAKLLGLGFPGGPAVEALARNGDPKAHDFPRPLLNRPGLDMSFAGLKTAVARASANAKSEAEKADICASFQAAICDVLAEKARRALEGFDAGAGDKRFVVAGGVASNKAIRAALETAATAQGARLIAPPLRHCTDNAAMIALAGAEHLAAGLCETDGLASSARPRWPLDEASAKADPVFGAGRRGAKA
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
Q0C5X3
A6ZZL8
MTC2_YEAS7
null
Saccharomyces
MGDHNLPDFQTCLKFSVTAKKSFLCMYRDSVSKEKLASSMPSTCDIQLKRAINDAYPGGGIKVTVLNSTTASLDSLATTHVKEFEIVIIPDINSLLQPDQAKLVKIMRDCTVAIEKAQSTRIFIGVVHWNNPVQPSGAAKDGDEAGKPAPKTRIFLPTSFRMGAWLKHKFWFACAPPYLDFESSTESSINTRANNSIGMAEEEKQEPESKRSIILNEEANLNDVFVGSTVRRYILDIMVHLRTHRLTYNAKAGGVYTNSLDDVVLLSRLIGLHSGKMFVSPSHVKEASRWYFPMHLELVQRSSMDSSLLYGSDPNLVDEMLEKLAKIKCEEVNEFENPLFLESLVVKNVLSKVVPPV
May be involved in telomere capping.
A6ZZL8
A0PQB8
SYP_MYCUA
Prolyl-tRNA synthetase
Mycobacterium
MITRMSELFLRTLRDDPADAEVPSHKLLIRAGYIRPVGPGLYSWLPLGLRVLRNIERVIREEMNAIGGQEILFPALLPRAPYETTNRWTEYGDGVFRLEDRRGNDYLLGPTHEELFTLTVKGEYNSYKDFPLTLYQIQIKYRDEARPRAGILRAREFVMKDSYSFDIDSGGLKAAYHAHREAYQRIFDRLRVRYVIVSAVSGAMGGSASEEFLAESPVGEDTFVRCVESGYAANVEAVVTARPESLPIDGQPDAVVHDTGETPTIATLVAWANEAGLGREVSAADTLKNVLMKIRQPGGEWELLAIGVPGDREIDEKRLAAALDPAEYVFLDDDDFGKYPFLVKGYIGPKALRSNDVRYLLDPRVVDGTSWITGADEPGRHVVGLVAGRDFTADGTIEAAEVREGDPAPDGAGQLVMARGIEIGHIFQLGRKYTDAFTADVLGEDGKPVRLTMGSYGIGVSRLVAVIAEQHHDNLGLRWPAEIAPFGVHLVIANKDAEARAGAIGLAGELDGLGVEVLLDDRQASPGVKFKDAELLGMPWVVVVGRGWADGVVELRDRFGGQTRELTVGDSLATDIAAAISG
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). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
A0PQB8
Q6D7B6
SYM_PECAS
Methionyl-tRNA synthetase
Pectobacterium
MTQVAKKILVTCALPYANGSIHLGHMLEHVQADIWVRYQRMRGNQVHFICADDAHGTPIMLKAQQMGIAPEQMIAAMSQEHQQDFAGFNISYDNYHSTHSEENRELSGLIYGRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKAADQYGDNCEVCGATYSTTELIEPKSAVSGATPEMRESEHFFFDLPAFSDMLQAWTRSGALQEQVANKMQEWFDSGLQQWDITRDAPYFGFEVPDAPGKYFYVWLDAPIGYMGSFKNLCDKRGDLNFDDFWKKDSDADLYHFIGKDIVYFHSLFWPAMLEGSGFRKPTNLFVHGYVTVNGAKMSKSRGTFIKAGTYLQHLDADCLRYYYAAKLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFISKRFDGKLADKLADAELYKTFTDAGASIAEAYSSRESGRAIREIMALADIANRYVDEQAPWVVAKVEGRDADLQAICSMGINLFRVLMTYLKPVLPALTQRTEAFLNTELSWDAITTPLLSHQVNPFKALFNRIDLDKVSAMVDASKEDMVTAQNVVSGPLADNPVQDTINFDDFAKVDMRIALIKQAELVDGSDKLLRLTLDLGGETRQVFSGIREAYPDPAKLEGRLTVMVANLAPRKMRFGISEGMVMAAGPGGKDIFLLSPDSGAQPGMQVK
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
Q6D7B6
Q13UP0
KYNB_PARXL
N-formylkynurenine formamidase
Paraburkholderia
MRTLWDITPAVDTATPVWPGDTPVGIERVWRMEAGSPVNVARLTLSPHTGAHTDAPLHYDAEGAAIGDVPLDAYLGRCRVIHCIGASPVVTPQHLTGSLDDLPPRVLLRTYRNAPTNVWDSAFCAVAPDTIDLLASRGVKLIGIDTPSLDPQESKTMDAHHRIRAHRMAILEGIVLDEVAAGDYELIALPLKLTTLDASPVRAILRALPESH
Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation.
Q13UP0
Q5R0C5
IF1_IDILO
Translation initiation factor IF-1
Idiomarina
MAKEDSIEMQGTVLDTLPNTMFRVELENGHVVTAHISGKMRKHYIRILTGDTVTVQLTPYDLTKGRIVFRAR
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.
Q5R0C5
Q74ZU2
TVP15_ASHGO
Golgi apparatus membrane protein TVP15
Eremothecium
MSENDQKGVKFIRALLVTTGAVATLGFLVQLSEVASEFLAAARACFGLPLSVLLVYLEFRPVPLLQQYASFYYSYMGRALLQLLLAVMLLPAGFFQVCAFTMLFMTGFICAALELSSSAPELPSFRNDGRALSIGAEEDDDMI
Golgi membrane protein involved in vesicular trafficking.
Q74ZU2
C4L191
MUTS_EXISA
DNA mismatch repair protein MutS
unclassified Exiguobacterium
MQEVHQTPMMKQYFSIKADYPDAFLFYRLGDFYELFFEDAQIVAKELELTLTSKNGKQAEHPIPMCGVPHHSAAIYIEQLIEKGFNVAICEQTEDPKATKGLVKREVIQVITPGTYMASLSEKENRYLVAISDVAGRFGIARGDVTTGESWLTTLSSEEAVLREIEGLLPNEVIVEDERLADLLRQTGIPLSIQVDKRESTLAQGAKDEAQRSAFELLFAYLTKTQKRSLDHLQPAVAYEVEQHMQLDANTARNLELFRSARSGERKGSLLSLLDETTTAMGGRLLKRWLEQPLYTEQGIRERQDAVENLVDDFMLRDQLQEELKRVYDIERLVAKVGYGTANARDLVQLRDTLERMPSVRSLLQTVKADRLQQIEQNLDSFETLSEQLRAALVDSPPISTKEGGMIRHGYSDELDELLEAKANGKSWIANLEQQERIATGIKSLKVGYNRVFGYYLEVTKANAKLLEEGRYERKQTLTNAERYITPELKEKEALILGAEEKSCTLEYDLFVALREEVKTYTKPLQQLARSLSELDVLLALAVVAEKREYVRPVTTSHVQIERGRHPVIETVLPRGEYVANDLTLDDTRQMLLITGPNMSGKSTYMRQFALIAILHQIGSFVPAEAAELPLFDRIFTRIGAADDLVSGQSTFMVEMTETRQAVTEATSNSLILLDEIGRGTSTYDGMALAQAIVEYIASSIGAKTLFSTHYHELTVLEDSIPSLENVHVRAIERDGRVVFLHEVHPGRADKSYGIHVAELAELPDSLIDRARTILSELESEATKPALNEQSAPPQVEEVSQLSLFESNDAVREQLLKLDLLAMNPIEAMQALYELQQTAKKG
This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity.
C4L191
Q891S2
DAPB_CLOTE
4-hydroxy-tetrahydrodipicolinate reductase
Clostridium
MEVYLMVRIMLVGCNGKMGRIITHCSKDFNDIEIVAGVDKSSTSNLDFPVFENIHSSSVECDVVLDFSRPSSLKSLISYCTEKKLPLVLCTTGYSKEELNLIEETSKNIPIFKSANMSIGINVINSLLKDISKKLYKDFDIEIIEKHHNQKVDSPSGTALLLADTIKDNVPEKLEYIYGRSGHSKRTKNEIGIHAIRGGSIVGDHDVIFAGIGECIEIKHTAISREVFAIGALKASAFMKGKPSGMYNMDCMLNS
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Q891S2
Q94J16
HFA4B_ORYSJ
Heat stress transcription factor 9
Oryza sativa
MEGGGGGGSLPPFLSKTYEMVDDPSTDAVVGWTPAGTSFVVANQPEFCRDLLPKYFKHNNFSSFVRQLNTYGFRKVDPEQWEFANEDFIKGQRHRLKNIHRRKPIFSHSSHSQGAGPLTDNERKDYEEEIERLKSDNAALSSELQNNTLKKLNMEKRMQALEEKLFVVEDQQRSLISYVREIVKAPGFLSSFVQQQDHHRKKRRLPIPISFHEDANTQENQIMPCDLTNSPAQTFYRESFDKMESSLNSLENFLREASEEFGNDISYDDGVPGPSSTVVLTELHSPGESDPRVSSPPTRMRTSSAGAGDSHSSRDVAESTSCAESPPIPQMHSRVDTRAKVSEIDVNSEPAVTETGPSRDQPAEEPPAVTPGANDGFWQQFLTEQPGSSDAHQEAQSERRDGGNKVDEMKSGDRQHLWWGKRNVEQITEKLGLLTSTEKT
Transcriptional regulator that specifically binds DNA of heat shock promoter elements (HSE).
Q94J16
Q5NUL3
FFAR4_HUMAN
Omega-3 fatty acid receptor 1
Homo
MSPECARAAGDAPLRSLEQANRTRFPFFSDVKGDHRLVLAAVETTVLVLIFAVSLLGNVCALVLVARRRRRGATACLVLNLFCADLLFISAIPLVLAVRWTEAWLLGPVACHLLFYVMTLSGSVTILTLAAVSLERMVCIVHLQRGVRGPGRRARAVLLALIWGYSAVAALPLCVFFRVVPQRLPGADQEISICTLIWPTIPGEISWDVSFVTLNFLVPGLVIVISYSKILQITKASRKRLTVSLAYSESHQIRVSQQDFRLFRTLFLLMVSFFIMWSPIIITILLILIQNFKQDLVIWPSLFFWVVAFTFANSALNPILYNMTLCRNEWKKIFCCFWFPEKGAILTDTSVKRNDLSIISG
Receptor for LCFAs decoupled from G-protein signaling. May signal through beta-arrestin pathway. After LCFAs binding, associates with beta-arrestin ARRB2 that may act as an adapter protein coupling the receptor to specific downstream signaling pathways, as well as mediating receptor endocytosis.
Q5NUL3
A6Q2V4
DAPA_NITSB
4-hydroxy-tetrahydrodipicolinate synthase
unclassified Nitratiruptor
MEKVKGAMTALITPFRNGKLDEEAYARLIQRQIDNAIDAVVPVGTTGESATLSHAEHKRCIEIAVEVCKGTSTKVMAGAGSNATHEAIDLAQFAQKAGADAILSVSPYYNKPTQEGLYQHYKALAESVDIPVLLYNVPGRTGVDIKPETVCRLFDDVNNIYGIKEATGSIERCVELLAKRPELYVISGDDAINYPIIANGGMGVISVTANLLPDKISMLVHAGLAGQFDTAKMINDELFDINKALFCESNPIPIKAAMYIAGLIDTLEYRLPLLEPSKEHMQLIEKTLAKYEVV
Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
A6Q2V4
A0RNM0
DAPE_CAMFF
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase
Campylobacter
MEVVEILKELLKFKSITPDDDGAMNFINMFMDGFDADFVDVNGIKNLILTKKFGDGVHLCFAGHIDVVPAGDGWDSDPFEPELKDGFVYARGAQDMKSGVAAFLCACKDATKFNGTLSIILTSDEEGDGIYGTLEALKFLKSRGNLPDFALVAEPTSSSTFGDTIKIGRRGSVNGVVTINGVQGHAAYPEKCVNPVHQLASVFSDFAGYELDSGSKYFGASKIVITDIRGGMEVVNVTPKSVKIMFNVRNSELTSCEDIKRYTEHIFNGFDFTLSLKESSKPFLTDESSKIVIQAQKSIENICKISPDLSTSGGTSDARYFAAFGVPVVEFGVVNDRIHAINERVLQSEVESLYLVFKDLIENFE
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.
A0RNM0
Q46J67
ATPE_PROMT
F-ATPase epsilon subunit
Prochlorococcus
MTLTLRVLAPDQSVFDDTADEIILPSTTGLLGVLPGHISMVTAIDFGVLRVLKNGNWDSIALTGGFAEVESNEVTVLVNKAEMGKNIDSGKAEAELEKAKNQLSQNKDQGNSPEKIKAQETLNKAKAWFQASKSD
Produces ATP from ADP in the presence of a proton gradient across the membrane.
Q46J67
B5FAQ4
NCPP_ALIFM
Nucleoside-triphosphate phosphatase
Aliivibrio
MKVIIASQNPAKIAAVESAFNLAFPNDTFSFEGVSVKSGVPDQPMSCEETKQGAINRVNNAKIKLPNCDYYVGLEAGIEGNSTFAWMIIDNGLTVGESRSSSLPLPPQVIDEVKKGKELGDVMDEQFNTDNIKQKGGAIGLLTNNLLTRTSVYQQALILALIPFLHPTRF
Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA/RNA precursor pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
B5FAQ4
A7FP52
HUTU_YERP3
Imidazolonepropionate hydrolase
Yersinia
MTTQNRFRDNEIRAPQGTQLTAKSWLTEAALRMLMNNLDPDVAENPKELVVYGGIGRAARNWECYDKIVESLINLNDDETLLIQSGKPVGIFKTHSNAPRVLIANSNLVPHWANWEHFNELDAKGLAMYGQMTAGSWIYIGSQGIVQGTYETFVEAGRQHFGGSLKGRWVLTAGLGGMGGAQPLAATLAGACSLNIECQQSRIDFRLKTRYVDEQATDLDDALARIEKYTATGVAVSIALCGNAAEILPELVRRGVRPDMVTDQTSAHDPLNGYLPKGWNWEEYRQRAQHEPALVINAAKISMAEHVEAMLAFHNMGIPTFDYGNNIRQMAHDMGVIRAFDFPGFVPAYIRPLFCRGIGPFRWVALSGNPDDIYKTDAKVKALIPDDAHLHHWLDMARERIRFQGLPARICWVGLGQRAKLGLAFNEMVRSGELSAPVVIGRDHLDSGSVASPNRETEAMQDGSDAVSDWPLLNALLNTASGATWVSLHHGGGVGMGFSQHSGMVVVCDGSDEAAERIARVLHNDPATGVMRHADAGYDIAVNCAQEQGLNLPMVAATQGKKS
Catalyzes the conversion of urocanate to 4-imidazolone-5-propionate.
A7FP52
Q4A5S7
RPOB_MYCS5
Transcriptase subunit beta
Mycoplasmopsis
MQKDKKNYKLRKFGPITERRDYSITKHSLPVGDILATSKKSYQDFINKKIEELLNEIYPIEASNKEASLEYEKKSVKFELPFKKAEHENLQIKTCKAKKTNFSMKVYITLKKVVSQTGVVKKEKILLGEIPYITSSGSFIINGSEKVIVSQLIRSPGAYFGVSVRNKQSEDLFNKLEILPRIGSWIEVSHKVTSANLDAIKIKIDKNKNINIVTFLASFGLLADDIRYLFGKNEVLEETIRKNKTIDITEFSRQEIMDLCQEKIFRIIRKGDRISEESKRSLLSGMLFDKKRYNLSKTGRYMLNNKLSLVERITNTYLAQKVVSHLGNTFDVGTYVTYEIAKEIQESFEAKAKDNKSNLHLEKIPNINPDDVYYKINKDNKSLNKRINIARIKIWPTKRAMDANETPSEVIGNDPKATEEHLLLSDIIAAISYYLNLTVGIGQDDDPDSLMNKRIVSVGELLEGELRIALLKLEKATRERMGAKEPDKITAKNVTNNKLITNQMKTFFNTSKLAQFMDQINPLAEISNKRRVTSLGPGGLNRDTAQFEVRDVHSTHYGRICPIETPEGPNIGLILNYAIYSTVNELGFLQTPYYKVNDGVVDYNDVRYLTSYEEIGYAFAQSSVHVNDKNEIIDEQITIKKDYNYIIGSPKDIDFLEVSSKQIVSVAAAAIPFLENNDANRALMGSNMQRQAVPLIEAEAPLVATGIEADIAKFSSYNIVANNDGEVIYVDGTKIQVRTAKKIDTYNLKNFEKSNQGTIIQQKPIVKVGDHVKEGDLLVDGSSFKDGEMALGKNLLVGFTTWNGYNFEDAIIINERLVKDDVLTSIYIEEQTIQFRISKSSEDIMTRDIPNVSKYSMRNLDEFGIIKVGSEVVAGDVLVGRISPKGEENPSQEEKLLNAIFNQRPQNYKDTSLKVKNGHNGTVIHVEVLSRENGDILEDGLDSIIKVYIAQKRKIKVGDKMAGRHGNKGVISIILPEEDMPHLEDGTPLDIMLNPQGVPSRMNIGQVLEMHLGMAAKKLGTKFVTPSFDGIKKETIEDLLQEANLDKSGKQVVIDPITGEKFDNPISVGVIYMLKLNHMVDDKMHARSVGPYSLITQQPLGGKSQNGGQRFGEMETWALESYGASNILQEILTYKSDDIYSRNLVYKALVNDSAIPNPGMPESFNVLSNELKGLLMKLGITETESNSDELIQHFDHLGVEHE
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Q4A5S7
Q5L0Y5
BSHC_GEOKA
Putative cysteine ligase BshC
Geobacillus thermoleovorans group
MEVREIPLPAATKLAADYITGAFPAESGFAYAQADDEAFCRRLAYLQGRTYDREGLADYLRAYHRRFSASVATMANIEKLRNERSVVIVGGQQAGLLTGPLYTIYKIITIIQLAKEQERKLGVPVVPLFWIAGEDHDIAEIDHVYVVEEGEVKKAAYPHKTNEKRMAADVLLDRMAAKEWIERVVKTYGETDVTNELLFFLSSCLDEARTFVDFFAAIVLRLFADHGLVVLNAGDAAVRPLERRFFAALIERHRDVTAAVLAQQEALRTLGYAPLIEIGRDAANLFYYDGRERSLLQYDEERGLFHNKAGTLVWTREELLELAETNPARLSNNVVTRPLMQEHLLPTLAFVAGPGEIAYWAELKEAFPLFDLEMPPVVPRLQATIVSRSLQTDLSDIGLEVADVLTGRLDEAKREWREATAQAPLASAFAKAKADIDAAHRPLRELGVAIDRGLEGLVAKNAAILQAQIEFLQHALERALLRKHETEWRKFWRIETSLRPNGALQERVWNVFYYINRYGFDFVEKLLAIRSPGNGMHKIVYM
Involved in bacillithiol (BSH) biosynthesis. May catalyze the last step of the pathway, the addition of cysteine to glucosamine malate (GlcN-Mal) to generate BSH.
Q5L0Y5
B0M3E6
PVK2_KARBO
CAPA-Periviscerokinin-2
Karoophasma
SGLQFAVLDGQGFIPFSRV
Mediates visceral muscle contractile activity (myotropic activity).
B0M3E6
Q89A27
EPMA_BUCBP
EF-P-lysine lysyltransferase
Buchnera
MNCNYLWKSSALLKNLHRRAKIIFEIRNYFFNLGILEVETPILSNYSVTDVNFIPFKTKLQITKKRMWLVPSPEYHMKRLLVQNIGAIYQISRSFRNNEFGGPYHNPEFTMLEWYSPYCNMFDFMKKVEKFLVFCLKVVQVKYISYQRAFIKYLNIDPLLAKKRELLDLINKFKFNHLISDCDSISTLLEILFTLKIEPNLNNKKLIFVYHYPADQAILAAINDNDSRVSDRFEVFFKGVELGNGFYELTDQAEHIRRFKLNNIQRRHKGICSVEVDQFFLKSLSRGLPPCSGIAIGLDRLIMLSLNLKTINEVIAFPIERC
With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P.
Q89A27
Q1KVY1
ATPF_TETOB
ATPase subunit I
Tetradesmus
MSFSFLFLGNLPLAEGFGINTNIFETNIINLAAVVAIVISFVGKNLSALLEDRRKTIVNNLQEASQRAAEAQERLNIAKNQLEVAKKKATEIREEGVFRATQEINNCVAQHEERLSKLEEFKQETVQFYQQKAFKQAYVYIISRIMSRVKERLNKGLDATYHVVVNNFYVSRFTEYNP
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Q1KVY1
A5CZ68
DNLJ_PELTS
Polydeoxyribonucleotide synthase [NAD(+)]
Pelotomaculum
MTQDLERARERAEELRREIEHHNYLYYVLDRPAITDAQYDRLMRELERLEKQFPALVTPYSPTQRVGGRPREGFAAVRHLSPMLSLANAFDERELRDFDRRVRQALPGEQVRYVVELKIDGLAVSLYYENGILVRGATRGDGDTGEDITENLKTVRSVPLRLRRPVPALEVRGEAFMPKEAFSRLNEGREEAGETLFANPRNAAAGSLRQLDPKITASRQLDLFVYGTGYGEWGRAVFPDGERTAPQEHAEVLELLKELGFKVNPEYRLFDRLDELVEYCLGWQARRFELPYAVDGLVIKVNSLAQQERLGATMKSPRWAVAYKFPPEQAVTKVKDIFVRVGRTGVLTPTAELEPVRLAGTTVSRATLHNEDIIREKDIRIGDKVLVQKAGDIIPEVVAVLKEERTGAEKAWAMPGRCPSCGAGVVRAEGEAAVRCTNMACPARLQEGLIHFASRDAMDIAGLGPAVIAQLVSAGLVGDPADLYALRYEDLVPLERLGPKSARNLLEAIEASKGRSLARLIFALGIRHVGERAAKILANHYQSLSGLMSATQEELVNIPEIGPKIAASIVEFFSNEQNRKVIDKLVKAGVNTLTEKVIREGGGPLNGKVFVLTGVLKDFSRQQAQELIESLGGRISSSVSRNTDFVVAGENPGSKYEKALTLGVKILDENEFRELTGRK
DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
A5CZ68
B8F6Q5
RL18_GLAP5
50S ribosomal protein L18
Glaesserella
MDKKVARIRRASRARHLMREQGATRLVVHRTPRHIYAQVIAPNGSEVLAAASTVEKVIKEQVKYTGNKEAAAVVGKIVAERALEKGIKAVAFDRSGFKYHGRVQSLADAAREAGLQF
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.
B8F6Q5
Q83HQ2
LGT_TROW8
Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase
Tropheryma
MHFYIPPPPISGFWLGPLYVHMYSVFMLAGALVLFELTNRRFIVLTGNREFTAFAVTSLLIPVILGARLWHVVSHTQMYEHQPFYKVFAIWQGGLGFIGGVFSGLICFFVIAKIKKVPPFTFLDALAPGILVALCFARLGNYFNGEVFGTETTLPWGLKLSHEGFKDLNVEKYFHPIFLYEIILNVFIIVILLVLEKRVFVKTVFPKGSVFAAFLVLYGLGRFALEPMRYNLQQNSFGLDLNYVGAAAMIIVGVLIACRHTIASGKLRNSGD
Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Q83HQ2
B4GDM5
EIF3M_DROPE
Transport and Golgi organization protein 7
Sophophora
MTSHPVFIDLSLDEQVQELRKYFKKLGAEISSEKSNKGVEDDLHKIIGVCDVCFKDGEPSQIDGILNSIVSIMITIPLDRGENIVLAYCEKMTKAPNQPLGKVCLQSLWRLFNNLDTASPLRYHVYYHLVQVAKQCEQVLEVFTGVDQLKTQFANCPPSSEQMQKLYRLLHDVTKDTNMELSSKVMIELLGTYTADNACVAREDAMKCIVTALADPNTFLLDPLLALKPVRFLEGDLIHDLLSIFVSDKLPSYVQFYEDHKEFVNSQGLNHEQNMKKMRLLTFMQLAESNPEMTFDTLTKELQITEDEVEPFVIQVLKTKLVRARLDQANRKVHISSTMHRTFGAPQWEQLRDLLQAWKENLSSVRDGLTNVSSAQLDLARTQKLIH
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
B4GDM5
Q2V0C9
CBS_APIME
Cystathionine beta-synthase
Apis
MEFKQPNRPSYCTWELNATNSPHTCRTKNGDYTKIMPDILTAIGQTPLIKLNNIPKSYGIKCEIYAKCEFLNPGGSVKDRIAYRMIQDAEDKGLLKPGCTIIEPTSGNTGIGLAMAAAVRGYKCIIVMPEKMSDEKISTLYALGAKIIRTPTEASWHSPEAHISVAQKLQKEIPNSIILDQYTNPGNPLAHYDQTAIEIWKQCEGKIDYLVAGAGTGGTISGIGRKLKELSPNIKIIAVDPKGSILDPSSDSQNEVGFYEVEGIGYDFIPTVLDRNVIDKWIKTEDNESLNAARMLIRQEGLLCGGSSGAALIAALKIAKDIPEEKRMVIILPDGIRNYLTKFVSEYWMETRGFLQPVCQNEMNKWWWNMKISNLSFDKQSLLKENTVTCQEAMHMLKNADSQLLVISDDNIHIKGVISLNKLTSYVISGIVKCTDFVDKAMVKQYVKVKHSATLGYISRVLEKEPYVIILDDEHDDAFIGIVNQFHILQFITKNGTSNNYLIN
Hydro-lyase catalyzing the first step of the transsulfuration pathway, where the hydroxyl group of L-serine is displaced by L-homocysteine in a beta-replacement reaction to form L-cystathionine, the precursor of L-cysteine.
Q2V0C9
Q184N9
ANMK_CLOD6
AnhMurNAc kinase
Clostridioides
MYSVGLMSGTSLDGIDAVLAEISGNGRNTKVKQIEFITLEISKDIKDEIRKCCIEEESSVDLICSLNFKLGYLFSKAVKSVCHKANFHIANLDFIASHGQTIFHIPRSYNNFVSSTLQIGEPAVIAYETNTKVISNFRVMDIAAGGEGAPLVPYSEFLLYSDKNKNLALQNIGGIGNITIIPKSCNIDDVFAFDTGPGNMIIDGVCQRLFNRKYDKNGYFASKGKINEEMLKDLMSHKYLSQAPPKSTGREVFGQVYLDNMLNKYKHVDKYDLIATVTMFTAKAIYYNYKNFILPKVNVDTLLIGGGGAHNLTLIGYIKELLLEVEVLTQDEYGYSSDAKEALAFVILGNETLNNSFSNVISATGAKNKVILGNITPKPFGGK
Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.
Q184N9
A5VC86
FABH_RHIWR
3-oxoacyl-[acyl-carrier-protein] synthase III
Rhizorhabdus
MRRAVVIGTGSALPRRQVSNAELARTVDTSDEWIVERTGIRNRYVAGEGETTSTLATEAARKAIEAAGIAPSDIGLIILATATPDQTFPASATMVQAALGIGDCVAFDVQAVCSGFLYALSVADSMIRGGSATHALVIGAETFSRILDWEDRTTCVLFGDGAGAVVLKAEEGGDRGVLATRLHADGRHNQLLYVDGGPSTTQTVGKLRMKGQEVFRHAVTNLAQVLREVMGDAGLTVDDIDWVVPHQANRRILDATARKLGLPAERVIVTVDQHANTSAASVPLALDVAVRDGRIKPGDLLVLEAMGGGFTWGAAAIRY
Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
A5VC86
B4EZ47
NUON_PROMH
NDH-1 subunit N
Proteus
MTITPEQLIAMLPLLVVILTVVVVMLSIAWRRDHFTIATLTATGFIIALGSLYYVNALGVVDVTTLYHVDGYSSFFTALTIIAGLGTVAFAYPWLEGYQDNKEEFYMLVAIAVIGGILLSSAHHLASMFIGIELLTLPLFGLIGYAFQQRPSLEASIKYMLLSAAASSFLLFGMALLYAEAGNLSFTAMGQSLSDSNIHKPLVLAGLGMMLVGIGFKLSLFPFQLWTPDVYQGAPAPTGAFLATASKIGIFAVVMRLFLEAPAADSETLRMILGFMAIASILFGNIMALTQKNVKRLLGYSSVSHLGYLLVALIVLQYSPILAQETAEIYLAGYLFASLGAFGAIAVASSPYNKGELESLEDYRGLFWRRPVAAVVMSLMMLSLAGVPITLGFIGKLYVILAGIDSSLWWLTGMVVLGSAIGLFYYLRAAAIVFLRKPDNDNAPAVTTTSQNMATLITLVCAIIVIVLGVWPQPLIELTRFAIIAPAIN
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
B4EZ47
Q5JDG3
GCST_THEKO
Glycine cleavage system T protein
Thermococcus
MVKRVHIFDWHKEHAKKVEEFAGWEMPIWYSSIKEEHLAVRNGVGIFDVSHMGEFIFRGKDALEFLQYVTTNDISKPPAISGTYTLVLNERGAVKDETLVFNMGNDTYMMVCDSDAFEKLDAWFNAIKRGIEKFGDIDLEIENKTYDMAMFSIQGPKARDLAKELFGIDINDLWWFQAKEVELDGIKMLLSRSGYTGENGFEVYFEDANPYHPDPSKRGEPEKALHVWKTILEAGEKYGIKPAGLGARDTLRLEAGYTLYGNETKEKQLLSTDIDEVTPLQANLDFAIFWDKEFIGKEALLKQKERGLPSKMVHFKMVDKGVPREGYKVYKDGELIGEVTSGTLSPLLGIGIGIAFVKPEYAVPGVEIEVEIRGKPKKAVTVAPPFYDPKKYGAFREE
The glycine cleavage system catalyzes the degradation of glycine.
Q5JDG3
A2STS4
TRMY_METLZ
tRNA (pseudouridine(54)-N(1))-methyltransferase
Methanocorpusculum
MLRFAVIGHKAVSTPDFSLNDMPGGAGRMDVLCRCINASFFLSHDLRRDTECFLILKGGEQADPANTVTLRFSGEKIKSLNPDERSAGALIKKALVTIPEEEYQRAAPGISIRKSGLAKLLEEHPFAVLDENGEDIRTAETLPENFILSDHQNFTEEEMELIKDLPKYSVGPRVLHADHTIIIILNEFDRRGEQA
Specifically catalyzes the N1-methylation of pseudouridine at position 54 (Psi54) in tRNAs.
A2STS4
Q96HA7
TONSL_HUMAN
Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor-like 2
Homo
MSLERELRQLSKAKAKAQRAGQRREEAALCHQLGELLAGHGRYAEALEQHWQELQLRERADDPLGCAVAHRKIGERLAEMEDYPAALQHQHQYLELAHSLRNHTELQRAWATIGRTHLDIYDHCQSRDALLQAQAAFEKSLAIVDEELEGTLAQGELNEMRTRLYLNLGLTFESLQQTALCNDYFRKSIFLAEQNHLYEDLFRARYNLGTIHWRAGQHSQAMRCLEGARECAHTMRKRFMESECCVVIAQVLQDLGDFLAAKRALKKAYRLGSQKPVQRAAICQNLQHVLAVVRLQQQLEEAEGRDPQGAMVICEQLGDLFSKAGDFPRAAEAYQKQLRFAELLDRPGAERAIIHVSLATTLGDMKDHHGAVRHYEEELRLRSGNVLEEAKTWLNIALSREEAGDAYELLAPCFQKALSCAQQAQRPQLQRQVLQHLHTVQLRLQPQEAPETETRLRELSVAEDEDEEEEAEEAAATAESEALEAGEVELSEGEDDTDGLTPQLEEDEELQGHLGRRKGSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCEGITPLHDALNCGHFEVAELLLERGASVTLRTRKGLSPLETLQQWVKLYRRDLDLETRQKARAMEMLLQAAASGQDPHSSQAFHTPSSLLFDPETSPPLSPCPEPPSNSTRLPEASQAHVRVSPGQAAPAMARPRRSRHGPASSSSSSEGEDSAGPARPSQKRPRCSATAQRVAAWTPGPASNREAATASTSRAAYQAAIRGVGSAQSRLGPGPPRGHSKALAPQAALIPEEECLAGDWLELDMPLTRSRRPRPRGTGDNRRPSSTSGSDSEESRPRARAKQVRLTCMQSCSAPVNAGPSSLASEPPGSPSTPRVSEPSGDSSAAGQPLGPAPPPPIRVRVQVQDHLFLIPVPHSSDTHSVAWLAEQAAQRYYQTCGLLPRLTLRKEGALLAPQDLIPDVLQSNDEVLAEVTSWDLPPLTDRYRRACQSLGQGEHQQVLQAVELQGLGLSFSACSLALDQAQLTPLLRALKLHTALRELRLAGNRLGDKCVAELVAALGTMPSLALLDLSSNHLGPEGLRQLAMGLPGQATLQSLEELDLSMNPLGDGCGQSLASLLHACPLLSTLRLQACGFGPSFFLSHQTALGSAFQDAEHLKTLSLSYNALGAPALARTLQSLPAGTLLHLELSSVAAGKGDSDLMEPVFRYLAKEGCALAHLTLSANHLGDKAVRDLCRCLSLCPSLISLDLSANPEISCASLEELLSTLQKRPQGLSFLGLSGCAVQGPLGLGLWDKIAAQLRELQLCSRRLCAEDRDALRQLQPSRPGPGECTLDHGSKLFFRRL
Component of the MMS22L-TONSL complex, a complex that promotes homologous recombination-mediated repair of double-strand breaks (DSBs) at stalled or collapsed replication forks . The MMS22L-TONSL complex is required to maintain genome integrity during DNA replication . It mediates the assembly of RAD51 filaments on single-stranded DNA (ssDNA): the MMS22L-TONSL complex is recruited to DSBs following histone replacement by histone chaperones and eviction of the replication protein A complex (RPA/RP-A) from DSBs . Following recruitment to DSBs, the TONSL-MMS22L complex promotes recruitment of RAD51 filaments and subsequent homologous recombination . Within the complex, TONSL acts as histone reader, which recognizes and binds newly synthesized histones following their replacement by histone chaperones . Specifically binds histone H4 lacking methylation at 'Lys-20' (H4K20me0) and histone H3.1 .
Q96HA7
Q5E702
NRDR_ALIF1
Transcriptional repressor NrdR
Aliivibrio
MHCPFCSATDTKVIDSRLVSDGHQVRRRRQCLACSERFTTFESAELVMPKVIKSNGNREPFDEDKLSGGLYRSLEKRPVSADLVELALNTIKSQLRATGEREVPSDMIGNLVMDQLKELDKVAYIRFASVYRSFEDIKEFGEEIAKLEK
Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
Q5E702
B1JBE9
CLPS_PSEPW
ATP-dependent Clp protease adapter protein ClpS
Pseudomonas
MHARSEIRLTFNQDRPQSNEDDGSGLAVQEAKPILQAPPMYKVVLFNDDYTPMDFVVEVLETFFSLNRELATKIMLTVHTEGRAVCGLFTRDIAETKAMQVNQYARESQHPLLCEIEKDG
Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation.
B1JBE9
A1KJW2
DTD_MYCBP
Gly-tRNA(Ala) deacylase
Mycobacterium tuberculosis complex
MRVLVQRVSSAAVRVDGRVVGAIRPDGQGLVAFVGVTHGDDLDKARRLAEKLWNLRVLAGEKSASDMHAPILVISQFTLYADTAKGRRPSWNAAAPGAVAQPLIAAFAAALRQLGAHVEAGVFGAHMQVELVNDGPVTVMLEG
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.
A1KJW2
Q115G6
NDHI_TRIEI
NDH-1 subunit I
Trichodesmium
MFKFLKQVSDYAKETFQSAKYIGQGLSVTFDHMSRRPVTVQYPYEKLIPSERFRGRIHFEYDKCIACEVCVRVCPINLPVVDWEFNKETKKKKLKHYSIDFGVCIFCGNCVEYCPSNCLSMTEEYELAAYDRHELNYDNVALGRLPYKVTNDPMVTPMRELAYLPKGVIDPHTVPHTSRRAGLRPEEILEQIEAEKTAAEKTAAEITDK
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Q115G6
Q21K23
CRCB_SACD2
Putative fluoride ion transporter CrcB
Saccharophagus
MTSAVPATSLILWLAVALGGALGALARYSVSIAWMPAQLKFPVATLTVNVLGSFLMGVFYVVIVEKAMLAPVWRHVIMIGFLGAFTTFSTFSIESLHLWQSGHWQIAISYVVANVVLSISAVVVAIVLTEKLV
Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Q21K23
Q764M5
STAT1_PIG
Signal transducer and activator of transcription 1
Sus
MSQWYELQQLDSKFLEQVHQLYDDSFPMEIRQYLAQWLENQDWEHAANDVSFATIRFHDLLSQLDDQYSRFSLENNFLLQHNIRKSKRNLQDNFQEDPIQMSMIICNCLKEERKILENAQRFNQTQSGNIQSTVMLDKHKELDSKVRNVKDKVMCIEHEIKTLEDLQDEYDFKCKTLQNREHDTNGVAKNDQKQEQMLLQKMYLMLDNKRKEVVHKIIELLNVTELTQKALINDELVEWKRRQQSACIGGPPNACLDQLQNWFTIVAESLQQVRQQLKKLEELEQKYTYEHDPITKNKQALWDRTFSLFQQLIQSSFVVERQPCMPTHPQRPLVLKTGVQFTVKLRLLVKLQKLNYNLKVKVLFDKDVSERNTVKGFRKFNILGTHTKVMNMEESTNGSLAAEFRHLQLKEQKNAGARTNEGPLIVTEELHSLSFETQLCQPGLVIDLETTSLPVVVISNVSQLPSGWASILWYNMLVAEPRNLSFFLNPPCARWSQLSEVLSWQFSSVTKRGLNVDQLNMLGEKLLGPTAGPDGLIPWTRFCKENINDKNFPFWLWIESILELIKKHLLSLWNDGCIVGFISKERERALLKDQQPGTFLLRFSESCREGAITFTWVERSQNGGEPYFHAVEPYTKKELSAVTFPDIIRNYKVMAAENIPENPLKYLYPNIDKDHAFGKYYSRPKEAPEPMELDGPKGTGYIKTELISVSEVHPSRLQTTDNLLPMSPEEFDEVSRMVGPVEFDVTWNKFSGTMNLD
Signal transducer and transcription activator that mediates cellular responses to interferons (IFNs), cytokine KITLG/SCF and other cytokines and other growth factors. Following type I IFN (IFN-alpha and IFN-beta) binding to cell surface receptors, signaling via protein kinases leads to activation of Jak kinases (TYK2 and JAK1) and to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize and associate with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of IFN-stimulated genes (ISG), which drive the cell in an antiviral state. In response to type II IFN (IFN-gamma), STAT1 is tyrosine- and serine-phosphorylated. It then forms a homodimer termed IFN-gamma-activated factor (GAF), migrates into the nucleus and binds to the IFN gamma activated sequence (GAS) to drive the expression of the target genes, inducing a cellular antiviral state. Becomes activated in response to KITLG/SCF and KIT signaling. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4.
Q764M5
Q3B316
AROK_CHLL3
Shikimate kinase
Pelodictyon
MGQDTITKQHSLIFLTGFSGSGKSTIGPLLANSLGYEFLDVDQAVEQRAGKPITRIFAEEGEAAFRELELQTLKTVAGEKEMVVSLGGGALQYDPSHAFIAGAGTLVYLKSSAANLAKRLVNKRDRPLLRGENGRKHSREELEEKIRRILEEREPRYQQAALTVQTDQKRIGSTVEELTRKIERLVRKAPQIGEDGQQPEQP
Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Q3B316
Q5Z880
HRD1_ORYSJ
RING-type E3 ubiquitin transferase HRD1
Oryza sativa
MIRLQTYAAFSLMATATAVYYAFSSREQFYPAMVYLSTSKICFVLLLNTGLVAMCVAWQLVKRLFLGTLREAEVERLNEQAWREVVEILFAVTIFRQDFSVSFLAMVAALLLVKALHWLAQKRVEYIETTPSVPMLSHARIVSFMLFLLVVDCLFLSNSLRSLIHKREASVAIFFSFEYMILATSTVSTFVKYIFYVSDMLMEGQWEKKAVYTFYLELISDLVHLSLYMLFFIAIFLNYGVPLHLIRELYETFRNFRIRIADYVRYRKITSNMNERFPDATADELNASDATCIICREEMTTAKKLLCGHLFHVHCLRSWLERQHTCPTCRAPILPPDNGRTAARPHGVHPGVQPVPGNGTPGSERAAGENISRRQAKLEAAASAASLYGRSFAYPPANNLNRYSTPPQSTSNGPQSGEASTSNQSPKGHATADPSAPTFYARGAVSSVTTTRELESSLQKAYENAIKSQIEMLQIQLQMFQHGATSSATNNENGEHTKSD
Probable component of the HRD1 ubiquitin ligase complex that mediates the rapid degradation of misfolded endoplasmic reticulum (ER) proteins, a process called ER-associated degradation (ERAD).
Q5Z880
P33619
KLK3_MACMU
Semenogelase
Macaca
MWVLVVFLTLSVTWIGAAPLILSRIVGGWECEKHSQPWQVLVASRGRAVCGGVLVHPQWVLTAAHCIRSNSVILLGRHNPYYPEDTGQVFQVSHSFPHPLYNMSLLKNRYLGPGDDSSHDLMLLRLSEPAEITDAVQVLDLPTWEPELGTTCYASGWGSIEPEEHLTPKKLQCVDLHIISNDVCAQVHSQKVTKFMLCAGSWMGGKSTCSGDSGGPLVCDGVLQGITSWGSQPCALPRRPSLYTKVVRYRKWIQDTIMANP
Hydrolyzes semenogelin-1 thus leading to the liquefaction of the seminal coagulum.
P33619
Q975R0
THI4_SULTO
Thiamine thiazole synthase
Sulfurisphaera
MDSNSIKVKQVDEVKISKYILKYTFQDWEDIVESDVVIVGAGPSGMTAAYYLAKAGLKTVVFERRLSFGGGIGGGAMLFHKIVIESPADEILKEMKIKLNKVEEGVYIVDSAEFMAKLAASAIDAGAKIIHGVTVDDVIFRENPLKVVGVAVEWTATQMAGLHVDPLFISAKAVVDATGHDAEVISVAARKIPELNIVIPGEKSAYSETAEELTVENTGMVAPGLYAAGMAVTEVKGLPRMGPIFGAMVLSGKRVAEIIIKDLRYS
Involved in the biosynthesis of the thiazole moiety of thiamine. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylate (ADT), an adenylated thiazole intermediate, using free sulfide as a source of sulfur.
Q975R0
Q66X22
NLR9B_MOUSE
NALP-delta
Mus
MAGSSGYGLLKLLQKLSDEEFQRFKELLREEPEKFKLKPISWTKIENSSKESLVTLLNTHYPGQAWNMMLSLFLQVNREDLSIMAQKKKRHKQTKYKKFMKTTFERIWTLETNTHIPDRNYHLIVEVQYKALQEIFDSESEPVTAIVAGTTGEGKTTFLRKAMLDWASGVLLQNRFQYVFFFSVFSLNNTTELSLAELISSTLPESSETVDDILSDPKRILFILDGFDYLKFDLELRTNLCNDWRKRLPTQIVLSSLLQKIMLPGCSLLLELGQISVPKIRHLLKYPRVITMQGFSERSVEFYCMSFFDNQRGIEVAENLRNNEVLHLCSNPYLCWMFCSCLKWQFDREEEGYFKAKTDAAFFTNFMVSAFKSTYAHSPSKQNRARLKTLCTLAVEGMWKELFVFDSEDLRRNGISESDKAVWLKMQFLQTHGNHTVFYHPTLQSYFAAMFYFLKQDKDICVPVIGSIPQLLGNMYARGQTQWLQLGTFLFGLINEQVAALLQPCFGFIQPIYVRQEIICYFKCLGQQECNEKLERSQTLFSCLRDSQEERFVRQVVDLLEEITVDISSSDVLSVTAYALQKSSKLKKLHLHIQKTVFSEIYCPDHCKTRTSIGKRRNTAEYWKTLCGIFCNLYVLDLDSCQFNKRAIQDLCNSMSPTPTVPLTAFKLQSLSCSFMADFGDGSLFHTLLQLPHLKYLNLYGTYLSMDVTEKLCAALRCSACRVEELLLGKCGISSKACGIIAISLINSKVKHLSLVENPLKNKGVMSLCEMLKDPSCVLQSLMLSYCCLTFIACGHLYEALLSNKHLSLLDLGSNFLEDTGVNLLCEALKDPNCTLKELWLPGCFLTSQCCEEISAVLICNRNLKTLKLGNNNIQDTGVRQLCEALSHPNCNLECLGLDLCEFTSDCCKDLALALTTCKTLNSLNLDWKTLDHSGLVVLCEALNHKRCNLKMLGLDKSAFSEESQTLLQDVEKKNNNLNILHHPWFEAERNKRGTRLVWNSRN
As the sensor component of the NLRP9 inflammasome, plays a crucial role in innate immunity and inflammation. In response to pathogens, including rotavirus, initiates the formation of the inflammasome polymeric complex, made of NLRP9, PYCARD and CASP1. Recruitment of proCASP1 to the inflammasome promotes its activation and CASP1-catalyzed IL1B and IL18 maturation and release in the extracellular milieu. The active cytokines stimulate inflammatory responses. Inflammasomes can also induce pyroptosis, an inflammatory form of programmed cell death. NLRP9 inflammasome activation may be initiated by DHX9 interaction with viral double-stranded RNA (dsRNA), preferentially to short dsRNA segments.
Q66X22
Q5ZEQ8
FJX1_XIPMA
Four-jointed protein homolog
Xiphophorus
MRALSANLFAVLLMCALASVFYVWSALENRLERHKRGSSVPDGGSFHQGPSEDHSAKTFRALLAVPVAQRQNSAGRSKAQNLTNPSAFVGSRDYHVNGDDERSAQREGPVKLGYPVDDGIFWSNWLEDVLPVRFTEGYAEAWRSKARTSPVVKLEPGCGRISNQLATFADGTKACVRYGINADQVQGETLTYYLASLLGITNLPPLVLSQLNGDSAQWVAVRTRINNLQWSDRAVVSLTEWISNLTGVVTPAPLRQESSGLLPALRCFENKTTAELLELMQWSDLIVFDYLTANFDRLVSNLFSLQWDPHVMERDTNNLLKTPHGDLVFIDNEAGLVHGFRVLNMWEKYHHSVLSSVCVFRKRTMQRVAELHRRRDSRQRLLELYRDSEPLSQELGFLSDEHAAVLQDRIDQLYKHIMQCKEKYNQL
May act as an inhibitor of dendrite extension and branching.
Q5ZEQ8
Q6C105
ATPF_YARLI
ATP synthase subunit b
Yarrowia
MPFARVGALSARHYSNQVDPKVKATSILDSIPGNNVLSKTGVLATGVLGSIYAISNELYIVNDESIVLGVFAAFVVVVAKLGGPGYTSWADGYIENMRNILNTTRDKHTDAVKERIGDVSKLKDVVKTTQDLFAVSKDTVKLEAEVFETKQQVVLAAEAKSVLDSWVRYENSVRQREQKLLTETVISKIEKDLKDPKFQQKILQQSVEDIEKLFAKA
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain . F-type ATP synthases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk . During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation . Part of the complex F(0) domain and the peripheral stalk, which acts as a stator to hold the catalytic alpha/ATP1(3)beta/ATP2(3) subcomplex and subunit a/ATP6 static relative to the rotary elements .
Q6C105
Q21XI7
TRPA_ALBFT
Tryptophan synthase alpha chain
Rhodoferax
MSRIARTFAGLKAQGRKALIPYVTAGFPFPDITPELMHAFVAGGADVIELGVPFSDPSADGPVIQKAGDKALAAGIGMVQVLDMVRTFRTRDASTPVVLMGYANPVERYNQKHDRHDGKSAFVLDAAAAGVDGVLIVDYPPEECEAFAAELKSAGLDLIFLLAPTSTDERMQQVARVASGYVYYVSLKGVTGSGALDTGAVEAMLPRIRAHVQVPVGVGFGIRDAATARTIGQVADAVVIGSKIIQLIDEQPRDQVGPVAQKFLCEIRTALDN
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Q21XI7
Q9UWU1
ARGDC_SACS2
Arginine decarboxylase alpha chain
Saccharolobus
MSEREVLQKINSPEGKEDRIIGKHVFGNLYDIDAERLNDKEFLEKLVLEAVDIAHMKLVEIKAWSFGGKKGGVSVIALVEESHIALHTWNEYNYATLDVYTCGEDSDPQSAFAHIVNALNPKRYQMFYADRSSQ
Specifically catalyzes the decarboxylation of L-arginine to agmatine. Is also able to decarboxylate L-canavanine, although less efficiently. Has no S-adenosylmethionine decarboxylase (AdoMetDC) activity.
Q9UWU1
P66861
SSRP_LISIN
Small protein B
Listeria
MPKGDGKLVAQNKKARHDYAIEETFEAGIVLQGTEIKSVRNARVNLKDSYARIDKGEIFLHNMHISPYEQGNRYNHDPLRTRKLLLHKKQISRLIGETKESGYSIVPLKMYIKDGYAKVLIGVARGKKKYDKRQDLKQKEAKRDIERAFKERQQ
Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation.
P66861
Q9PJN4
RPOA_CHLMU
Transcriptase subunit alpha
Chlamydia
MSDNSHNLLYNKFELPESVKMSPVEGAAGGIDKVARFVADPLEKGMGHTLGSALRRALLIGLEAPAIVSFSMTGVLHEYMAVEGIIEDVTNIVLNLKGSLLKKYPLQDCEGGRASQKLRATISIDASDLAAAGGQKAITLGDLLQEGTFEAVNPEHVIFTVTRPMQLDVMLRVAFGRGYTPSERIVLEEREMNEIVLDAAFSPVVLVNYFVEDTRVGQDTDFDRLILQVETDGRVAPKEAVAFATQILSKHFSVFEKMDEKRIVFEEAISVEKENKDDILHKLVLGINEIELSVRSTNCLSNANIETIGELVIMPEPRLLQFRNFGKKSLCEIKNKLKEMKLELGMDLSQFGVGLDNVKEKMKWYAEKIRSSKNTKG
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Q9PJN4
Q2S289
MDH_SALRD
Malate dehydrogenase
Salinibacter
MKVTVIGAGNVGATVAECVARQDVAKEVVMVDIKDGMPQGKALDMRESSPIHGFDTRVTGTNDYGPTEDSDVCIITAGLPRSPGMSRDDLLAKNTEIVGGVTEQFVEGSPDSTIIVVANPLDVMTYVAYEASGFPTNRVMGMAGVLDTGRFRSFIAEELDVSVRDVQALLMGGHGDTMVPLPRYTTVGGIPVPQLIDDARIEEIVERTKGAGGEIVDLMGTSAWYAPGAAAAEMTEAILKDNKRILPCAAYCDGEYGLDDLFIGVPVKLGAGGVEEVIEVDLDADEKAQLKTSAGHVHSNLDDLQRLRDEGKIG
Catalyzes the reversible oxidation of malate to oxaloacetate.
Q2S289
B6JNH4
NADD_HELP2
Nicotinate mononucleotide adenylyltransferase
Helicobacter
MNTMNSVLKYKELALYGGSFDPLHKAHLAIIDQTLELLPFAKLIVLPAYQNPFKKPCFLDAKTRFKELERALKGMPRVLLSDFEIKQERAVPTIESVIFFQKLYRPKTLYLVIGADCLRHLSSWTNATELLKRVELVVFERIGYEEIQFKGHYHPLKGIDAPISSSAIRASLGV
Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
B6JNH4
A5W9S6
HISZ_PSEP1
ATP phosphoribosyltransferase regulatory subunit
Pseudomonas
MATVDRWLLPDGIEEVLPPEAARIEIARRQVLDLFQSWGYELVVTPHIEYLESLLTGAGQDLDQRTFKVVDPQSGRLMGFRADFTPQVARIDAHTLRREGPSRLCYAGSVLHAQPRALSTSRSPIQLGAELYGDASPTSDVEVISLMLATLQLADVPDVHMDLGHVGIYRGLARAAGLSGAVEQQLFDAMQRKAVDEVQALTADLPKDLGSMLRALVELCGGREVLAEARVRLGRAPASVLAALDDLLAIADRLASRYPDLPLYFDLGELRGYHYHTGVVFAVFVPGEGQSIAQGGRYDDIGADFGRARPATGFSTDLKTLVTLGRAEVVLPTGGIWMPDSGDAALWQQVCQLRNEGQRVVQALPGQPLSAALEADCDRQLIQQDGRWQVLPLAQ
Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
A5W9S6
Q6PQZ3
INSI2_PIG
Insulin-induced gene 2 protein
Sus
MAEGETKSPGPKKCGPYISSVTSQSVNLMIRGVVLFFIGVFLALVLNLLQIQRNVTLFPPDVIASIFSSAWWVPPCCGTASAVIGLLYPCIDRHLGEPHKFKREWSSVMRCVAVFVGINHASAKVDFDNNIQLSLTLAALSIGLWWTFDRSRSGFGLGVGIAFLATLVTQLLVYNGVYQYTSPDFLYVRSWLPCIFFAGGITMGNIGRQLAMYECKVIAEKSHQE
Oxysterol-binding protein that mediates feedback control of cholesterol synthesis by controlling both endoplasmic reticulum to Golgi transport of SCAP and degradation of HMGCR. Acts as a negative regulator of cholesterol biosynthesis by mediating the retention of the SCAP-SREBP complex in the endoplasmic reticulum, thereby blocking the processing of sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2. Binds oxysterol, including 22-hydroxycholesterol, 24-hydroxycholesterol, 25-hydroxycholesterol and 27-hydroxycholesterol, regulating interaction with SCAP and retention of the SCAP-SREBP complex in the endoplasmic reticulum. In presence of oxysterol, interacts with SCAP, retaining the SCAP-SREBP complex in the endoplasmic reticulum, thereby preventing SCAP from escorting SREBF1/SREBP1 and SREBF2/SREBP2 to the Golgi. Sterol deprivation or phosphorylation by PCK1 reduce oxysterol-binding, disrupting the interaction between INSIG2 and SCAP, thereby promoting Golgi transport of the SCAP-SREBP complex, followed by processing and nuclear translocation of SREBF1/SREBP1 and SREBF2/SREBP2. Also regulates cholesterol synthesis by regulating degradation of HMGCR: initiates the sterol-mediated ubiquitin-mediated endoplasmic reticulum-associated degradation (ERAD) of HMGCR via recruitment of the reductase to the ubiquitin ligase RNF139.
Q6PQZ3
B3DRT8
HIS6_BIFLD
ImGP synthase subunit HisF
Bifidobacterium
MSLAVRVIPCLDVDAGRVVKGVHFENLKDAGDPVELAAEYYRQGADEITFLDVTASSSHRNTMIDVVSCTAEQVFIPMTVGGGVRTPEDVDSLLRCGADKVGVNTAAINDPSLISRVADRFGNQVLVLSVDARREKGEQHTQSGFEVTTMGGRKSTGIDAIWWVKRAEQLGAGEILLNSMDADGTKEGFDLEMIRAVRKEVKIPIIASGGAGKVEDFPPAIEAGADAVLAASVFHYGILTIADVKAELKKHGYTVR
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
B3DRT8
Q1H190
RNH_METFK
Ribonuclease H
Methylobacillus
MSSNVIEIYADGACKGNPGPGGWGAWLSFAGHEKELWGGELVTTNNRMELTAVIRALEALKRQCSVRIYTDSVYVQKGITEWVHSWKARNWLTSDRKPVKNVDLWKALDSLVQQHQVEWVWVKGHAGNVGNERADALANKGVDQVLGREVV
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Q1H190
A5WBF8
DNAJ_PSYWF
Chaperone protein DnaJ
Psychrobacter
MSKRDFYEVLGVDRSADEREIKKAYRKLAMKYHPDRNSDDPDAEEKFKEASMAYEVLSDKEKRSAYDRMGHAAFENGMGGGGFGGAGAGNFQDIFGDIFGNFGDIFGQSRGGGGRQRRGSDLRYVIELSLEEAVRGCKKEISFTAPAPCETCDGKGAKNASDIQTCSTCGGHGQVRMQQGFFAVQQTCPNCGGSGQEIKNPCNDCHGTGVKDKSRTLEVSIPAGVDDGDRVRLAGEGEAGGAGVQNGDLYVEVRVKEHPVFKRQGADLYMDVPVSITDAALGKEVEIPTLDGKVKIKVAEGTQSGKLLRVRGKGVTPVRTTMKGDLICRIMVETPVNLTREQKDLLRQFQDTLDGDSKHHQSPKKKSFFEKLGDLFD
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
A5WBF8
A8F7Z9
OTC_PSELT
Ornithine carbamoyltransferase
Pseudothermotoga
MAINLTGRSLLTLLEYTPEEISFLLDLSAQVKRESRARIVHKRFAGKTLAMIFEKRSTRTRMAFETAFAEEGGHPIFLSIQDIQLGAKESIEDTARVLGRMVDAIMFRGYKQETVETLAKYSGVPVYNGLTDVYHPTQVLADLMTTQEVFGKLKGIKLVFMGDGRNNMANSLMIGCAKMGMHYVVCSPAELRPDENLMQTCLTIAKETDSKIEVIDDPEKAVDGADVIYTDVWASMGEESKQQERERLLRPYQVNEVLMRKTGKKDTIFLHCLPAVKGQEVTFDVIEGKQSRVWDEAENRKHTIKALMIATLL
Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
A8F7Z9
A5DAF0
ARGJ_PICGU
Arginine biosynthesis bifunctional protein ArgJ beta chain
Meyerozyma
MVVNKGIRLLSTKAARFVPSGGVYPKGFVVGGIHCGVKKDGKSPDLAVLHNTFGQDANAAAVFTKNKFKAAPVQVSAATIKQKNGVGINSIIVNSGNANAVTGQKGMEDARAMAMVTDSVFGDHKDSTLVMSTGVIGNKLPIDNILSGIPKLESQVGDSHDHWLACANAICTTDTFPKLVSKSFEINGNTYTMAGVAKGAGMICPNMATLLGFFVTDAPVSAKALQQILSYATDRSFNSISVDGDMSTNDTIVAIANGAAGGDLIDNNSSCAESYFELQKEVTSFAQKLAQLVVRDGEGATKFITLKVKDALSYKDAKSIASSIANSSLFKTAMFGKDANWGRILCAIGYSDVSTAQSIIPDRTSVTFVPTDGSEPLPLLVDGEPESVDEARAAQILELEDLEIEIDLGTGGGQEAKFWTCDLSHEYVTINGDYRS
Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate.
A5DAF0
Q1LT61
FABA_BAUCH
Trans-2-decenoyl-[acyl-carrier-protein] isomerase
Candidatus Baumannia
MIEKREFYSKEDLIASSRGELFGERGPQLPAHQMLMMDQVVKITKYGGHYNKGFMEAELDIKPDMWFFCCHFIGDPVMPGCLGLDAMWQLVGFYLGWIGGKGKGRALGVGEVKFIGQILPSAKKVTYRIHFRRIIHRQLLMGMADGEVICDGKIIYTATDLKVGLFQDPTILS
Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length.
Q1LT61
Q0ZJ25
PSBD_VITVI
Photosystem Q(A) protein
Vitis
MTIALGKFTKDESDLFDIMDDWLRRDRFVFVGWSGLLLFPCAYFALGGWFTGTTFVTSWYTHGLASSYLEGCNFLTAAVSTPANSLAHSLLLLWGPEAQGDFTRWCQLGGLWTFVALHGAFGLIGFMLRQFELARSVQLRPYNAIAFSAPIAVFVSVFLIYPLGQSGWFFAPSFGVAAIFRFILFFQGFHNWTLNPFHMMGVAGVLGAALLCAIHGATVENTLFEDGDGANTFRAFNPTQAEETYSMVTANRFWSQIFGVAFSNKRWLHFFMLFVPVTGLWMSALGVVGLALNLRAYDFVSQEIRAAEDPEFETFYTKNILLNEGIRAWMAAQDQPHENLIFPEEVLPRGNAL
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.
Q0ZJ25
P08240
SRPRA_HUMAN
Docking protein alpha
Homo
MLDFFTIFSKGGLVLWCFQGVSDSCTGPVNALIRSVLLQERGGNNSFTHEALTLKYKLDNQFELVFVVGFQKILTLTYVDKLIDDVHRLFRDKYRTEIQQQSALSLLNGTFDFQNDFLRLLREAEESSKIRAPTTMKKFEDSEKAKKPVRSMIETRGEKPKEKAKNSKKKGAKKEGSDGPLATSKPVPAEKSGLPVGPENGVELSKEELIRRKREEFIQKHGRGMEKSNKSTKSDAPKEKGKKAPRVWELGGCANKEVLDYSTPTTNGTPEAALSEDINLIRGTGSGGQLQDLDCSSSDDEGAAQNSTKPSATKGTLGGMFGMLKGLVGSKSLSREDMESVLDKMRDHLIAKNVAADIAVQLCESVANKLEGKVMGTFSTVTSTVKQALQESLVQILQPQRRVDMLRDIMDAQRRQRPYVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHTRRLSALHPPEKHGGRTMVQLFEKGYGKDAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVGNEAVDQLVKFNRALADHSMAQTPRLIDGIVLTKFDTIDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAALMKA
Component of the signal recognition particle (SRP) complex receptor (SR) . Ensures, in conjunction with the SRP complex, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system . Forms a guanosine 5'-triphosphate (GTP)-dependent complex with the SRP subunit SRP54 . SRP receptor compaction and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER .
P08240
P48256
YCF12_CYAPA
Photosystem II reaction center protein Ycf12
Cyanophora
MGNLDLEIIAQLTVVTLTLLAGPVIVFLLSVRKGNL
A core subunit of photosystem II (PSII).
P48256
P0A2B5
RIMM_SALTY
Ribosome maturation factor RimM
Salmonella
MSKQLAAQVPAEPVVLGKMGSSYGIRGWLRVFSSTEDAESIFDYQPWFIQKAGQWQQVQLESWKHHNQDLIIKLKGVDDRDAANLLTNCEIVVDSSQLPALEEGDYYWKDLMGCQVVTAEGYDLGKVIDMMETGSNDVLVIKANLKDAFGIKERLVPFLDGQVIKKVDLATRTIEVDWDPGF
An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Probably interacts with S19. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
P0A2B5
D5C1K8
TMCA_NITHN
tRNA(Met) cytidine acetyltransferase TmcA
Nitrosococcus
MHPILFPPTLDNIRKITASLVAAAKASGHRRALVLSGDREWCLQAAQVSLASTSLEPVLWIAAQAPENAWRMEAAKAHRSLGQEVDAIVFDAYSGFDLDAFGIITGAIRGGGLLLLLTPPLAAWPSFNDPEHARIVTAPYEVTEVTGRFLKRLVRILREAEGVIIIEQGKILPSVPFAAPARAETGGNPPSPGDSACRTEDQGRAVEAIVKVVTGQRRRPVVLTSDRGRGKSAALGIAAARLLQRGLKHIIVTGPRLDAVEPVFRHAQRLLPQATVSRAALHLPEAGMEFAPPDDLIRTSRPADLLLVDEAATIPTPLLERLLQGYSRIAFATTIHGYEGTGRGFALRFHRVLDEKTRGWKGLRLETPIRWRSGDPLEHFVFRALLLDATAAPDSAVASARPETVAVERLDRDALVRDEATLSELFGLLVLAHYQTRPYDLRHLLDGPNLSVYVMRYRGHVVATALLAAEGGFVEETARGIWEGRTRPHGHLLPESLAAHLGLAQAPRLHCARIMRIAVHPAVQGQGLGTHLVDTIIRETGGEGLDYLGSSFGATVELLRFWERLDFLPVRLSVKRGATSGAHSAIVLHPLSSSGQALVKRARERFLVHLPHQLADPLRELEPQLAAWLLRRGDPAGPLPLDSQDWSDVLAFAFGRRVYEVCIGPIWKLTWGALAAPESATLLGEVERNALIVKVLQKRSWQEAAAALELSGRAQVIEVLRRTLRPLVLHFGNEAVRREAERLAGG
Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP).
D5C1K8
Q5SLM3
CBP1_THET8
TthCP1
Thermus
MTPEAAYQNLLEFQRETAYLASLGALAAWDQRTMIPKKGHEHRARQMAALARLLHQRMTDPRIGEWLEKVEGSPLVQDPLSDAAVNVREWRQAYERARAIPERLAVELAQAESEAESFWEEARPRDDWRGFLPYLKRVYALTKEKAEVLFALPPAPGDPPYGELYDALLDGYEPGMRARELLPLFAELKEGLKGLLDRILGSGKRPDTSILHRPYPVEAQRRFALELLSACGYDLEAGRLDPTAHPFEIAIGPGDVRITTRYYEDFFNAGIFGTLHEMGHALYEQGLPKEHWGTPRGDAVSLGVHESQSRTWENLVGRSLGFWERFFPRAREVFASLGDVSLEDFHFAVNAVEPSLIRVEADEVTYNLHILVRLELELALFRGELSPEDLPEAWAEKYRDHLGVAPKDYKDGVMQDVHWAGGLFGYFPTYTLGNLYAAQFFQKAEAELGPLEPRFARGEFQPFLDWTRARIHAEGSRFRPRVLVERVTGEAPSARPFLAYLEKKYAALYG
Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues, but not Pro. Has lower activity with substrates ending with Gly or Glu.
Q5SLM3
Q7RYU8
HAT1_NEUCR
Histone acetyltransferase type B catalytic subunit
Neurospora
MSGDDDWWTSSNEALLVSLVTPSDTGVKTLDTFHPEYTNNIFGEKEQIFGYKGLRINLQYNASDMLPNLKVSYKKKYQPTADEEALDINEVLSEFLPEIAFQKQSDFETRLKSIPDNWTPPGTLVTSFTNKDGEYEVYSGKITDPAVKQLLNRIQILVPFFVDGGTPIDMEDPDVDRWTIYFLYNKRPLLNQPDKFSYHFAGYSTLYRYYAFQPPAESESKTPTDTPTFSVDGDFDLDTLPCRTRISQFIIIPPFQQKGLGSRLYSIIYQQYLKHEPTIELTVEDPNEAFDDMRDLADLAFLSKQPEFQALKIDTSVEIPEEGKAPSNIVDQAAWEACRKKFKIVPRQFARVLEMYLMSQLPESVRPGLGAPEDEDYEEQSGRSKSKGHEKALPKPTPEDEHTYRLWMMLVKRRLYVHNRDALGQLELKERREELAKVFAGVEFDYARLLIKAEEQGKLAQADGETAGDQVPATPSAANGKRKLDEVEQAEGTAAASSKKAKVESGHA
Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-12' of histone H4 which is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.
Q7RYU8
P80655
MTRB_METMA
N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit B
Methanosarcina
MSIVRIAPEINLVMDTESGTVTQERKDSIQYSMEPVFERVDKLDAIADDLVNSLSPSKPLLNTWPGRENTSYIAGIYSNSFYGIIVGLAFSGLLALIIYITRLMGGVV
Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.
P80655
Q0IDE5
ISPH_SYNS3
4-hydroxy-3-methylbut-2-enyl diphosphate reductase
unclassified Synechococcus
MDTHAFKRSLHHSDRYNRRGFGRADEVAGSLEQAYQSSLIGSIRDNGYSLTHGRLKVRLAEAFGFCWGVERAVAMAYETRRHYPQERIWITNEIIHNPSVNDHLREMDVLFISVEGGVKDFSGVATGDVVILPAFGATVQEMQLLNERGCHIVDTTCPWVSKVWTTVEKHKKQSFTSIIHGKVKHEETLATSSFAGTYLVVLDLEEARLVADYILGKGNRESFMERFSKACSPGFDPDRDLEHLGVANQTTMLKSETEEIGRLFERTMLSKYGPTDLNEHFLAFNTICDATQERQDAMFSLVDETVDLMVVIGGYNSSNTTHLQEIAVSRGIRSFHIDTPERIHTDNSIEHKPLGEELTVEELFLPSGPVTVGITSGASTPDRVVEHVIQRLIALSEN
Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
Q0IDE5
B2IM47
COAD_STRPS
Pantetheine-phosphate adenylyltransferase
Streptococcus
MSDKIGLFTGSFDPMTNGHLDIIERASRLFDKLYVGIFFNPHKQGFLPIENRKRGLEKAVKHLGNVKVVSSHDELVVDVAKRLGATCLVRGLRNASDLQYEASFDYYNHQLSPDIETIYLHSRPEHLYISSSGVRELLKFGQDIACYVPESILEEIRNEKKD
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
B2IM47
B3PS53
MNME_RHIE6
tRNA modification GTPase MnmE
Rhizobium
MAMLNDTIYALSSGAPPSGVSVIRVSGTLTRDILFQLVGSVPAARTASYRTIRTRYDQPVDSGLVLFFPGPNSFTGEDAAELQIHGSKAVLAALFRELGDIPGVRMAMEGEFSRRAFENGKLDLVEVEGLADLIGAETEMQRRLAVEQSAGGVSAIYDSWAERLTRARALIEAELDFPDEDDVPGSVSDMVWADMARLRHDIALHLEAASAGEIIRDGFKVVIAGAPNAGKSSLMNALAKREVAIVTDIAGTTRDVLHVDLDIDGYLVKLYDTAGLREAEDRVEIEGVRRARVALRDADLVLLLVDMSNPIIPADLEQALPHVTVGTKKDLIETASDRYDLQISTTTGEGLPELRDLIGRVVKERYGGQSLAIPSRQRHKDSLAKCLAALDAAISQGSANLELRTEQLRLAAEYLGRITGRVDVEQLLDVIFSEFCIGK
Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
B3PS53
A6H742
PLSI_BOVIN
Plastin-1
Bos
MENSTTTISREELEELQEAFNKIDIDNSGYVSDYELQDLFKEASLPLPGYKVREIVEKILAVADNNKDSRISFEEFVSLMQELKSKDISKTFRKIINKREGITAIGGTSSISSEGTQHSYSEEEKVAFVNWINKALENDPDCKHLIPMNPNDDSLFKSLADGILLCKMINLSEPDTIDERAINKKKLTPFTISENLNLALNSASAIGCTVVNIGAQDLTEGKPHLVLGLLWQIIKVGLFADIEISRNEALIALLKEGEDLEELMRLSPEELLLQWVNYHLTNAGWPTISNFSHDIKDSRAYFHLLNQIAPKGDRDDGPAIAIDLTGFSEKNDLKRAEFMLQEADKLGCRQFVTPADVVSGNPKLNLAFVANLFNTYPGLHKPDNNDIDVNLLEGESKEERTFRNWMNSLGVNPYINHLYSDLADALVIFQLYEMIRVPVDWSHVNKPPYPALGGNMKKIENCNYAVELGKNKAKFSLVGIAGQDLNEGNSTLTLALVWQLMRRYTLNVLSDLGEGEKVNDAIIIEWVNQTLKSANKNTFISSFKDKSISTSLPVLDLIDAIAPNAVRQEMIKREDLSDEDKLNNAKYAISVARKIGARIYALPDDLVEVKPKMVMTVFACLMGKGLNKIK
Actin-bundling protein. In the inner ear, it is required for stereocilia formation. Mediates liquid packing of actin filaments that is necessary for stereocilia to grow to their proper dimensions.
A6H742
Q9ZRR8
CHS1_CASGL
Naringenin-chalcone synthase
Casuarina
MVTVEEVRKAQRAEGPATVLAIGTATPPNCLDQSTYPDYYFRITNSEHKTELKEKFQRMCDKSMIKKRYMYLTEEILKEHPNMCAYMAPSLDARQDMVVVEIPKLGKEAAVKAIKEWGQPKSKITHLVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAGGTVLRLAKDLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFGDGAAAIIVGADPLPEVEKPLFEVVSTAQTILPDSDGAIDGHLREVGVTFHLLKDVPGLISKNIEKSLVEAFQPLGISDWNSLFWIAHPGGPAILDQVEEKLALKPEKLGATRHVLSEYGNMSSACVLFILDEMRRKSAEKGLKTTGEGLDWGVLFGFGPGLTVETVVLHSLTT
The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin.
Q9ZRR8
Q5L8C5
RL18_BACFN
50S ribosomal protein L18
Bacteroides
MTTKIERRIKIKYRVRNKVSGTAARPRMSVFRSNKQIYVQIIDDLSGKTLAAASSLGMTEKLPKKEVAAKVGEIIAKKAQEAGITTVVFDRNGYLYHGRVKEVADAARNGGLKF
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.
Q5L8C5
B3CN84
DAPB_WOLPP
4-hydroxy-tetrahydrodipicolinate reductase
unclassified Wolbachia
MKIRVGVIGCLGRMGKKILNELITNTKVEIAGAVARLGSEYIGLDIGPIVGNNCNLGIKITSSISEVFESSDVVIDFTTKECMLECLKAAVKFKKPLVSGTTGIEGLNLKDYAAKVPILWSANMSIGVNVLLKLVKEAAKLLGNEYDVEIWEMHHNLKKDSPSGTAIEFGKAVANAAKVDFELNQYSHNNSNIRGKGGIGFAVSRGGGVIGDHSVMFVNYDERVELNHKAIDRTTFARGAVQAAIWLCENKTPGLYSMQDLV
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
B3CN84
Q2HAX7
ARGJ_CHAGB
Arginine biosynthesis bifunctional protein ArgJ beta chain
Chaetomium
MAMAGCNGFFLHQLRQPRLQLARQLGRTPSRAYSAPSNGSIPAAKKKYVPTKGTYPLGFRTSGTIVGVKPSNTTKPDLALLTSDAPCVAAAVFTKNKFQAAPVTFSRNLLERRKNQGIQSVIINSGCANAVTGKGGLEDATKMAQEADKCTGQNESTIVMSTGVIGQRLPIDKILNKVPSAHGALGGSHDHWLAAAKAICTTDTFPKLMSRTFALPSSPGVEYRIAGMTKGAGMIHPNMATLLGVIATDAPITSAALPSALKHAVDRSFNSITIDGDTSTNDTVALFANGAAGGKEVAEGTPDYDAFRAVLTDFAAELAQLVVRDGEGATKFVTVRVTESASEEAARRIASTIARSPLVKTALYGKDANWGRILCATGYSLISEPGQPINDVPEIAPEKTNVSFIPTDGTAELKLLVNGEPEKVDEARAAEILELEDLEILVRLGQGDKQATYWTCDYSHEYITINGDYRT
Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate.
Q2HAX7
A5IHG9
HEMH_LEGPC
Protoheme ferro-lyase
Legionella
MRRGLLLLNLGTPDNADIRAVKLYLREFLTDKRVIDLPTIPRYILVYCLILPFRSPKSAQAYQSIWTEKGSPLLYHSQNLVTKLQSALKDEYKIALGMRYGTPSITTALAELKDCHSLTILPLFPQYSSAATGSAIEKTLSYLANQEIIPSIKIIRDFYQRPEYIQAQAKIMKPYIKDNFHVLFSYHGIPERHIHKSGCDTLCPQTCTPIYDKNQACYRAQCYQTSLLLAKELQLGTHQYTTAFQSRLGKTPWIKPYTDEIFAELISKGIKNIVVSCPSFVADCLETLEEIGIRAKEQWEKLGGEQFILTPCMNDHPEWIKAIHSIVNEQI
Catalyzes the ferrous insertion into protoporphyrin IX.
A5IHG9
Q3C1H8
PSAA_NICSY
PsaA
Nicotiana
MIIRSPEPEVKILVDRDPVKTSFEEWARPGHFSRTIAKGPDTTTWIWNLHADAHDFDSHTSDLEEISRKVFSAHFGQLSIIFLWLSGMYFHGARFSNYEAWLSDPTHIGPSAQVVWPIVGQEILNGDVGGGFRGIQITSGFFQIWRASGITSELQLYCTAIGALVFAALMLFAGWFHYHKAAPKLAWFQDVESMLNHHLAGLLGLGSLSWAGHQVHVSLPINQFLNAGVDPKEIPLPHEFILNRDLLAQLYPSFAEGATPFFTLNWSKYADFLTFRGGLDPVTGGLWLTDIAHHHLAIAILFLIAGHMYRTNWGIGHGLKDILEAHKGPFTGQGHKGLYEILTTSWHAQLSLNLAMLGSLTIVVAHHMYSMPPYPYLATDYGTQLSLFTHHMWIGGFLIVGAAAHAAIFMVRDYDPTTRYNDLLDRVLRHRDAIISHLNWACIFLGFHSFGLYIHNDTMSALGRPQDMFSDTAIQLQPVFAQWIQNTHALAPGATAPGATASTSLTWGGGDLVAVGGKVALLPIPLGTADFLVHHIHAFTIHVTVLILLKGVLFARSSRLIPDKANLGFRFPCDGPGRGGTCQVSAWDHVFLGLFWMYNAISVVIFHFSWKMQSDVWGSVSDQGVVTHITGGNFAQSSITINGWLRDFLWAQASQVIQSYGSSLSAYGLFFLGAHFVWAFSLMFLFSGRGYWQELIESIVWAHNKLKVAPATQPRALSIIQGRAVGVTHYLLGGIATTWAFFLARIIAVG
PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin.
Q3C1H8
P17021
ZNF17_HUMAN
Zinc finger protein KOX10
Homo
MNLTEDYMVFEDVAIHFSQEEWGILNDVQRHLHSDVMLENFALLSSVGCWHGAKDEEAPSKQCVSVGVSQVTTLKPALSTQKAQPCETCSSLLKDILHLAEHDGTHPKRTAKLYLHQKEHLREKLTRSDEGRPSFVNDSVHLAKRNLTCMQGGKDFTGDSDLQQQALHSGWKPHRDTHGVEAFQSGQNNYSCTQCGKDFCHQHTLFEHQKIHTEERPYECSECGKLFRYNSDLIKHQRNHTGERPYKCSECGKAFSLKYNVVQHQKIHTGERPYECSECGKAFLRKSHLLQHQRIHTRPRPYVCSECGKAFLTQAHLVGHQKIHTGERPYGCNECGKYFMYSSALIRHQKVHTGERPFYCCECGKFFMDSCTLIIHQRVHTGEKPYECNECGKFFRYRSTLIRHQKVHTGEKPYECSECGKFFMDTSTLIIHQRVHTGEKPYECNKCGKFFRYCFTLNRHQRVHSGERPYECSECGKFFVDSCTLKSHQRVHTGERPFECSICGKSFRCRSTLDTHQRIHTGERPYECSECGKFFRHNSNHIRHRRNHFGERSFECTECGRVFSQNSHLIRHQKVHTRERTYKCSKCGKFFMDSSTLISHERVHTGEKPYECSECGKVFRYNSSLIKHRRIHTGERPYQCSECGRVFNQNSHLIQHQKVHTR
May be involved in transcriptional regulation.
P17021
Q9RTN2
PSRP_DEIRA
Pyruvate, water dikinase regulatory protein
Deinococcus
MSGWGMPRPVFIVSDHTGLTAENIARALLTHFPGQPLRYLRRPFTSDAQAAQAVVSEVEALAASGERPLIFTTTTQPDVLEALQTAPAQVFDLLTENLRLLEGEFAEPPQLGAGGHHDMQDSEAYLSRMEALDFALATDDGIGDKQYGLSDVILVGVSRAGKTPTSLFLALQHGIRASNYPLAEDDFEREGLPAPLEQYRSKLFGLTIDPRRLHAIRTQRKPGSKYASIEQCEYEVRRASALFARLGLPVKDTTSASVEEIAAGVLALLRQSGRLEG
Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the phosphoenolpyruvate synthase (PEPS) by catalyzing its phosphorylation/dephosphorylation.
Q9RTN2
B8HPJ7
ATPL_CYAP4
Lipid-binding protein
unclassified Cyanothece
MDPQIASASVLAAALAIGLAAIGPGIGQGNASGQAVEGIARQPEAEGKIRGTLLLTLAFMESLTIYGLVIALVLLFANPFAG
Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.
B8HPJ7
A0LRN7
RS5_ACIC1
30S ribosomal protein S5
Acidothermus
MATAGRRGGAASERRERRESRRQEASPEKSNFLERVVTINRVAKVVKGGRRFSFTALVVVGDGNGMVGVGYGKAREVPAAIAKGVEEAKKHFFTVPRVQGTIPHPVIGEAAAGVVLLRPASPGTGVIAGGPVRAVLECAGVRDVLSKSLGSDNAVNIVHATVKALRALVPPEKVAVRRGLPLEEVAPPALLRAKAEAGV
Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body.
A0LRN7
Q0SS19
SCPB_CLOPS
Segregation and condensation protein B
Clostridium
MSDINQIEFSEISKKDELKSIIESLLFVSGEPLALKDICRIVEEDFKYVEDLMRELMNIYNGDSSRGIKIISLNGTYQLVTKTKNSEYIQKLLKKNVRQSLSQASLESLAIICYKQPITRVEIDEIRGVKSESAIQRLVEKNLVEETGRLEVPGRPILYGTTDEFLRHFALNDLGDLPSIELFEENNEVSDMVEE
Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpA that pull DNA away from mid-cell into both cell halves.
Q0SS19
Q4WEL6
SLX1_ASPFU
Structure-specific endonuclease subunit slx1
Aspergillus subgen. Fumigati
MDDTQIEHPRPIPIFYCCYLLRSTVRHASLYIGSTPNPARRLIQHNGVVKGGARRTAAEKLRPWEMVLVVEGFMSRLAALQFEWAWQNPWYSRHLRSEESSALAEVKHRRMRKAKSEDPEFLDSNCDSAKSRVKGTPKKSKRRHRPPRSLDTYFSDLHRLLRSTYFSHWPLKIRFFSGDIYQSWKAWYDRVDVRLRSPVKVILDGSCPEISAHTGGNDTRFGGVENAKITYAAIRDYIEKAIFLLDDPKDVRCHVCQGQIVPTEELTTVCPQAECHCTCHLLCLSRKFVDAALEPNQIVPKHGICPACEATIEWPLMMKELSFRSRAKQELLEILKRKRRVDRKQGAVTGEVESSSRRTVSVDLDDRFGQHAEDEFLLDEDWWEGLAAESDSDTDLRLKPLSKAAPKLETVIEDSECDDADIL
Catalytic subunit of the slx1-slx4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
Q4WEL6
Q73FC6
MCSB_BACC1
Protein-arginine kinase
Bacillus cereus group
MSLDKIMNEAISPWMKGDGPDSDIVLSSRIRLARNFKKYQFSTMQNEEEAKLIQELFKKEFINKTVEPFGEFELLKMNELTPLQRRVLVEKHLISPNLAGTEYGACLLSESEHISVMLNEEDHIRIQCLFSGLQLSEALQSANQIDNWIEKEVEYAFDESLGYITSCPTNVGTGLRASVMIHLPGLVLTKRISRIIQVIQKLGLVVRGIYGEGSEALGNIFQVSNQMTLGKSEEDIIADLKSVIQQIIQQEKMARELIVQNSSIELEDKVYRSYGILANSRLIQSAEAANCLSDLRLGIDLGYIKGISRNILTELMVLTQPGILQQYAGGPLGPEERDYRRATLIRERLRIEKN
Catalyzes the specific phosphorylation of arginine residues in a large number of proteins. Is part of the bacterial stress response system. Protein arginine phosphorylation has a physiologically important role and is involved in the regulation of many critical cellular processes, such as protein homeostasis, motility, competence, and stringent and stress responses, by regulating gene expression and protein activity.
Q73FC6
P74165
BMGDS_SYNY3
UDP-glucose:1,2-diacylglycerol 3-beta-D-glucosyltransferase
unclassified Synechocystis
MPQFPWKDNDAELSPLEAFLAEWDDPEAEEEDFRNDFFRGSEGRRKKAAVMLMAIWTVVITLHYWVWGSWLVWALTGALSLQALRLMKATPEEAPPLLTGDASTVPYPQVCLMVAAKNEEAVIGKIVQQLCSLDYPGDRHEVWIVDDNSTDRTPAILDQLRQQYPQLKVVRRGAGASGGKSGALNEVLAQTQGDIVGVFDADANVPKDLLRRVVPYFASPTFGALQVRKAIANEAVNFWTRGQGAEMALDAYFQQQRIVTGGIGELRGNGQFVARQALDAVGGWNEQTITDDLDLTIRLHLHQWKVGILVNPPVEEEGVTTAIALWHQRNRWAEGGYQRYLDYWRWICTQPMGWKKKLDLFSFLLMQYLLPTAAVPDLLMALWQRRFPLLTPLSYLAIGFSCWGMYYGLKRLTPSEGESPWQQMPALLARTIGGTIYMFHWLIIMPAVTARMAFRPKRLKWVKTVHGAATEDALELKQS
Glucosyltransferase involved in the biosynthesis of the non-bilayer-forming membrane lipid beta-monoglucosyldiacylglycerol which contributes to regulate the properties and stability of the membrane. Catalyzes the transfer of a glucosyl residue from UDP-Glc to diacylglycerol (DAG) acceptor to form the corresponding beta-glucosyl-DAG (1,2-diacyl-3-O-(beta-D-glucopyranosyl)-sn-glycerol). It can only use UDP-Glc as sugar donor. Two types of DAG (dipalmitoyl-DAG (DPDAG) and 1-oleoyl-2-palmitoyl-DAG (OPDAG)) can be used as sugar acceptors, but OPDAG is preferred.
P74165
P28310
DEFA3_MOUSE
Defensin-related cryptdin-3
Mus
MKTLVLLSALVLLAFQVQADPIQNTDEETKTEEQPGEDDQAVSVSFGDPEGSSLQEESLRDLVCYCRKRGCKRRERMNGTCRKGHLMYTLCCR
Probably contributes to the antimicrobial barrier function of the small bowel mucosa.
P28310
Q9RY65
RL27_DEIRA
50S ribosomal protein L27
Deinococcus
MAHKKGVGSSKNGRDSNPKYLGVKKFGGEVVKAGNILVRQRGTKFKAGQGVGMGRDHTLFALSDGKVVFINKGKGARFISIEAAQTEVAAD
Binds the 5S and 23S rRNAs and also the tRNA in the P site.
Q9RY65
Q6P3V2
Z585A_HUMAN
Zinc finger protein 585A
Homo
MPANWTSPQKSSALAPEDHGSSYEGSVSFRDVAIDFSREEWRHLDPSQRNLYRDVMLETYSHLLSVGYQVPEAEVVMLEQGKEPWALQGERPRQSCPGEKLWDHNQCRKILSYKQVSSQPQKMYPGEKAYECAKFEKIFTQKSQLKVHLKVLAGEKLYVCIECGKAFVQKPEFIIHQKTHMREKPFKCNECGKSFFQVSSLFRHQRIHTGEKLYECSQCGKGFSYNSDLSIHEKIHTGERHHECTDCGKAFTQKSTLKMHQKIHTGERSYICIECGQAFIQKTHLIAHRRIHTGEKPYECSNCGKSFISKSQLQVHQRVHTRVKPYICTEYGKVFSNNSNLVTHKKVQSREKSSICTECGKAFTYRSELIIHQRIHTGEKPYECSDCGKAFTQKSALTVHQRIHTGEKSYICMKCGLAFIQKAHLIAHQIIHTGEKPHKCGHCGKLFTSKSQLHVHKRIHTGEKPYMCNKCGKAFTNRSNLITHQKTHTGEKSYICSKCGKAFTQRSDLITHQRIHTGEKPYECNTCGKAFTQKSHLNIHQKIHTGERQYECHECGKAFNQKSILIVHQKIHTGEKPYVCTECGRAFIRKSNFITHQRIHTGEKPYECSDCGKSFTSKSQLLVHQPVHTGEKPYVCAECGKAFSGRSNLSKHQKTHTGEKPYICSECGKTFRQKSELITHHRIHTGEKPYECSDCGKSFTKKSQLQVHQRIHTGEKPYVCAECGKAFTDRSNLNKHQTTHTGDKPYKCGICGKGFVQKSVFSVHQSSHA
May be involved in transcriptional regulation.
Q6P3V2
Q9M1C2
CH101_ARATH
10 kDa chaperonin 1, chloroplastic
Arabidopsis
MASSFITVPKPFLSFPIKTNAPTLPQQTLLGIRRNSFRINAVSTKWEPAKVVPQADRVLVRLEVLPEKSSGGVLLPKSAVKFERYLTGEVVSVGSEVGEVEPGKKVLFSDMSAYEVDFGTEDAKHCFCKESDLLAIVQ
Functions as co-chaperone for protein folding in chloroplasts.
Q9M1C2
Q2S1Q1
RL11_SALRD
50S ribosomal protein L11
Salinibacter
MAAPVEQTIKLQIKGGQANPAPPIGPALGQHGVNIMEFCKAFNSRTEDRMGTLLPVEITVYADRSFDFIVKSPPASVLLKQKADIETAAGDPLRDDAGTVTWDDCLDIADQKLQDLNAHTVEKGASMVAGTARSMGITVEGKPAHE
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
Q2S1Q1
Q9R0C0
BL1S6_MOUSE
Syntaxin 13-interacting protein
Mus
MSVPEPPPPDGVLTGPSDSLEAGEPTPGLSDTSPDEGLIEDFPVDDRAVEHLVGGLLSHYLPDLQRSKRALQELTQNQVVLLDTLEQEISKFKECHSMLDINALFTEAKHYHAKLVTIRKEMLLLHEKTSKLKKRALKLQQKRQREELEREQQREKEFEREKQLTAKPAKRT
Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. May play a role in intracellular vesicle trafficking, particularly in the vesicle-docking and fusion process.
Q9R0C0
P04844
RPN2_HUMAN
Ribophorin-2
Homo
MAPPGSSTVFLLALTIIASTWALTPTHYLTKHDVERLKASLDRPFTNLESAFYSIVGLSSLGAQVPDAKKACTYIRSNLDPSNVDSLFYAAQASQALSGCEISISNETKDLLLAAVSEDSSVTQIYHAVAALSGFGLPLASQEALSALTARLSKEETVLATVQALQTASHLSQQADLRSIVEEIEDLVARLDELGGVYLQFEEGLETTALFVAATYKLMDHVGTEPSIKEDQVIQLMNAIFSKKNFESLSEAFSVASAAAVLSHNRYHVPVVVVPEGSASDTHEQAILRLQVTNVLSQPLTQATVKLEHAKSVASRATVLQKTSFTPVGDVFELNFMNVKFSSGYYDFLVEVEGDNRYIANTVELRVKISTEVGITNVDLSTVDKDQSIAPKTTRVTYPAKAKGTFIADSHQNFALFFQLVDVNTGAELTPHQTFVRLHNQKTGQEVVFVAEPDNKNVYKFELDTSERKIEFDSASGTYTLYLIIGDATLKNPILWNVADVVIKFPEEEAPSTVLSQNLFTPKQEIQHLFREPEKRPPTVVSNTFTALILSPLLLLFALWIRIGANVSNFTFAPSTIIFHLGHAAMLGLMYVYWTQLNMFQTLKYLAILGSVTFLAGNRMLAQQAVKRTAH
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation . N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
P04844
Q2JTQ2
RL7_SYNJA
50S ribosomal protein L7/L12
unclassified Synechococcus
MASERVQKILEELKALSLLEASELVKAIEEAFGVSAAAPAGGMVMAAPVAAAAAPAPAAAPEPVEEQTAFDVILEAVPADKKIAVLKVVRELTGLGLKDAKDLVEAAPKPVKEGIPKEEANEIKKKLEEAGATVKVK
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
Q2JTQ2
P16333
NCK1_HUMAN
SH2/SH3 adaptor protein NCK-alpha
Homo
MAEEVVVVAKFDYVAQQEQELDIKKNERLWLLDDSKSWWRVRNSMNKTGFVPSNYVERKNSARKASIVKNLKDTLGIGKVKRKPSVPDSASPADDSFVDPGERLYDLNMPAYVKFNYMAEREDELSLIKGTKVIVMEKCSDGWWRGSYNGQVGWFPSNYVTEEGDSPLGDHVGSLSEKLAAVVNNLNTGQVLHVVQALYPFSSSNDEELNFEKGDVMDVIEKPENDPEWWKCRKINGMVGLVPKNYVTVMQNNPLTSGLEPSPPQCDYIRPSLTGKFAGNPWYYGKVTRHQAEMALNERGHEGDFLIRDSESSPNDFSVSLKAQGKNKHFKVQLKETVYCIGQRKFSTMEELVEHYKKAPIFTSEQGEKLYLVKHLS
Adapter protein which associates with tyrosine-phosphorylated growth factor receptors, such as KDR and PDGFRB, or their cellular substrates. Maintains low levels of EIF2S1 phosphorylation by promoting its dephosphorylation by PP1. Plays a role in the DNA damage response, not in the detection of the damage by ATM/ATR, but for efficient activation of downstream effectors, such as that of CHEK2. Plays a role in ELK1-dependent transcriptional activation in response to activated Ras signaling. Modulates the activation of EIF2AK2/PKR by dsRNA. May play a role in cell adhesion and migration through interaction with ephrin receptors.
P16333
Q609A9
RECR_METCA
Recombination protein RecR
Methylococcus
MRQAGAIAELIEALRCLPGVGPKTAQRMTLHLLQRDRDAAGRLSEALRQALEKVGLCAQCRTLTEHSLCEYCASPGRDRSLLCIVESPAEVLAISRSTGYKGLFFVLNGRLSPLDGIGPEELGLDVLEQRLKDDGVAELILATNTTVEGEATAHYLSDMARRHGVRTTRIAHGIPFGGELEYVDGATLSHAFDGRKDF
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.
Q609A9
Q127X5
NUOD_POLSJ
NDH-1 subunit D
unclassified Polaromonas
MAEIKNYTLNFGPQHPAAHGVLRLVLELDGEVIQRADPHIGLLHRATEKLAESKTYIQSLPYMDRLDYVSMMSNEQAYCLAIEKLLGVDVPIRAQYIRVMYAEITRLLNHLLWLGAHGFDCGAMNILIYCFREREALFDMYEAVSGARMHAAYFRPGGVYRDLPDTMPQYRVSKIKNAKAIAALNENRQGSLLDFIDDFVAKFPRLVDEYETLLTDNRIWKQRTVGVGVVSPERALNLGFTGPMLRGSGFAWDLRKQQPYDVYDRMDFDIPVGKTGDCYDRYLVRIEEMRQSNRIIKQCIDWLRVNPGPVITSNHKVAAPDRESMKTNMEELIHHFKLFTEGFHVPEGEAYAAVEHPKGEFGIYIVSDGANKPYRLKIRPPGFPHLAAMDEMSRGHMIADAVAVIGTMDIVFGEIDR
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Q127X5
Q63798
PSME2_RAT
Proteasome activator 28 subunit beta
Rattus
MAKPCGVRLSGEARKQVDAFRQNLFQEAEDFLCTFLPRKIISLSQLLQEDSLNVADLSSLRAPLDIPIPDPPPKDDEMETEQEKKEVPKCGFLPGNEKLLALLALVKPEVWTLKEKCILVITWIQHLIPKIEDGNDFGVAIQEKVLERVNAVKTKVEAFQTAISKYFSERGDAVAKASKDTHVMDYRALVHERDEAAYGALRAMVLDLRAFYAELHHIISSNLEKIVNPKGEEKPSMY
Implicated in immunoproteasome assembly and required for efficient antigen processing. The PA28 activator complex enhances the generation of class I binding peptides by altering the cleavage pattern of the proteasome.
Q63798
C4L0S2
LUTA_EXISA
Lactate utilization protein A
unclassified Exiguobacterium
MPNVALFVTCLSDTLFPSVGQATVELLEHLGCEVTFPFEQTCCGQPAYNSGYHEETKKIAKHMIETFEQADAEYIVGPSGSCVMMMRDYPHLFQDDPVWRPRAEAHAAKTFELTQFIVDVLEVTDVGAKFPAKATYHASCHMTRLLGIEAAPGKLLGNVDGLTMVPLANVHNCCGFGGTFSVKMPDVSVQMVDEKVDSILQSGAEVLIGADASCLMNIGGRLHKQGHPIKVMHIAEVLNEGVKQA
Is involved in L-lactate degradation and allows cells to grow with lactate as the sole carbon source.
C4L0S2