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Full Name
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sequence
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2.75k
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5.51k
AlphaFoldDB
stringlengths
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10
B2S9F3
RIMP_BRUA1
Ribosome maturation factor RimP
Brucella
MTEQVQANETETPVAVADERIIRETGIDAKVAGIVEPVINTLGFRLVRVRLSGLNGQTLQIMAERPDGTMTVDDCELVSRTVAPVLDVEDPISGKYHLEISSPGIDRPLVRKSDFSDWAGHIAKVETSIVHEGRKKFRGRIVVGEADSVTIESDQISYGNEPVVRIPFDLISDARLVLTDDLIRDALRKDKALREGRIPGDDLGAEPEDVASTETQEKK
Required for maturation of 30S ribosomal subunits.
B2S9F3
Q10X61
PCYA_TRIEI
Phycocyanobilin:ferredoxin oxidoreductase
Trichodesmium
MLKTSIPSQGIQQNPLVCQLANSIEAVWQRYLNLEPYYLPADLGYVEGRLEGEKLIIQNKCYQTAQFRKLHLELATIGPKLDILHCVMFPRISYPLPIFGTDLVGARGQISAAVVDISPQSQDRKLPEVYNYQLQALPIKEFAHPRQLPQWGEIFSEFCLFIRPTGLEEEQKFISIVESYLEIHCQQAIAQKPVSPEQQLEILKAQHHYCTQQRQNDKTRRVLEKAFGPEWTDYYLTTVLFDSPN
Catalyzes the four-electron reduction of biliverdin IX-alpha (2-electron reduction at both the A and D rings); the reaction proceeds via an isolatable 2-electron intermediate, 181,182-dihydrobiliverdin.
Q10X61
B4LFW2
QTRT2_DROVI
Queuine tRNA-ribosyltransferase domain-containing protein 1
Drosophila
MKFVLKSISKNSGRLGQLRIKQSKELQTPLLLQTTKGGSIPYLSAEVFDLVSQEHQQVLQLTLSTMDQMSESLAQWNRSLSDYVGYPGYNTLLLLRDPCETTPTGGNDRDVVPLFTRHGKESLTAARYMDMVANFAPDVYQGLCDADTNPESTKKRVQKSVDRTERFMELCYEQHSKLARLKDSTLLAPIVGGYSTFARTQSIKHARQQPAGSYGGYILEGFHTNGLAATELKAAQLLPIVEHCVQQLEEEQPRLMPGAYTPLLLLELIRLGVDVFDSSYAYCAATNYKALTFSYVRDKAEHAAFLDVTDEAIKEDFKPLLEDCSCLSCQKHTRAYIHHLYKTHELLGTILLMIHNLHHYMCFFEAIRASMAADQLPELIEHVRMQNTTAEVNYRIEPNNKVVGKAAMGKGFIAAAV
Non-catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
B4LFW2
A7FYL4
GATC_CLOB1
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C
Clostridium
MSVSKKDVEYVAELARLEFKEEEKDSFVNDLNKILNYMEKLDELNTDDVDIVVNPYYIENKYREDNVEKSMELKEVIDNAPESLEEYVIVPKVID
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
A7FYL4
Q87ST0
LEUD_VIBPA
Isopropylmalate isomerase
Vibrio
MSGFKQHTGLVVPLDAANVDTDAIIPKQFLQKVSRLGFGKHLFHDWRFLDDAGERPNPEFVMNAPRYQGASILLARENFGCGSSREHAPWALADYGIKAMIAPSFADIFYGNSINNQMVPVRLTEQEVDELFQFVEANEGAQIEVDLEALKVRANGKEYDFEIDEFRRHCLLNGLDNIGLTLQHEDKIAEYEANIPSFLR
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Q87ST0
O07293
BLO18_PSEAI
Penicillinase
Pseudomonas
MQRSLSMSGKRHFIFAVSFVISTVCLTFSPANAAQKLSCTLVIDEASGDLLHREGSCDKAFAPMSTFKLPLAIMGYDADILLDATTPRWDYKPEFNGYKSQQKPTDPTIWLKDSIVWYSQELTRRLGESRFSDYVQRFDYGNKDVSGDPGKHNGLTHAWLASSLKISPEEQVRFLRRFLRGELPVSEDALEMTKAVVPHFEAGDWDVQGKTGTGSLSDAKGGKAPIGWFIGWATRDDRRVVFARLTVGARKGEQPAGPAARDEFLNTLPALSENF
Has a broad substrate profile, hydrolyzes amoxicillin, ticarcillin, cephalothin, ceftazidime, cefotaxime, and aztreonam, but not imipenem or cephamycins.
O07293
Q92051
CAHZ_DANRE
Carbonate dehydratase
Danio
MAHAWGYGPADGPESWAESFPIANGPRQSPIDIVPTQAQHDPSLKHLKLKYDPATTKSILNNGHSFQVDFVDDDNSSTLAGGPITGIYRLRQFHFHWGSSDDKGSEHTIAGTKFPCELHLVHWNTKYPNFGEAASKPDGLAVVGVFLKIGAANPRLQKVLDALDDIKSKGRQTTFANFDPKTLLPASLDYWTYEGSLTTPPLLESVTWIVLKEPISVSPAQMAKFRSLLFSSEGETPCCMVDNYRPPQPLKGRKVRASFK
Reversible hydration of carbon dioxide.
Q92051
A9IVC5
GLYA_BART1
Serine hydroxymethyltransferase
Bartonella
MTQQENDTQKRFFNDNLQIVDDAIFNAMRGEFERQQHEIELIASENIVSRAVLEAQGSVLTNKYAEGYPRKRYYGGCQFVDLVEDLAIERAKQLFGAAFANVQPNSGSQMNQAVFLALLQPGDTFMGLDLNAGGHLTHGSSVNMSGKWFDVVSYGVRQEDQIIDMDEVERLAKERKPKLIIAGGSSYPRFWDWERFREIADEIGAHLLVDMSHIAGLVAGGVHPSPVPHAHIVTTTTHKSLRGPRGGLILTNDEALSKKINSAIFPGLQGGPLMHVIAAKAVAFGEALHPSFKSYSVNVVANAKTLAKTLQSNGFNIVSGGTDNHLLLVDLRSKNLTGKRAELALGRAHITCNKNGIPFDPETPSITSGIRLGSPAATTRGFLEKEFVQVAHLIAEVLDGLRNAKSDEDNHAVEMAVKKKVEDITNQFPLYSYLSTR
Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
A9IVC5
B7K4A4
AMPA_RIPO1
Leucyl aminopeptidase
Rippkaea orientalis
MDIRGINTPFLDWTGDALALGIFEEGTQITGELSQLDGKLTGTVQELIQEAEFEGKAGTKAVTRVGSNSPIRKVMLVGLGKAEDLQLNSVREAAGAIARLAKLEKVKTLGINLPVVNNDGAKTASAIAEGILLALHQDNRFKSDPQENALKLENVDILGCGEATEAINRAQTLSSGVILARELVNSPANTITPVTFAETAQEIAQTSGLTCEILEQEDCEKLGMGSFLGVAKASDLPPKFIHLTYKPSGTPKKKLAIVGKSLTFDCGGLNLKVAGASIEMMKMDMGGGAATLGAAKVIGQLKPDVEVHFICAATENMISGRAIHPGDILTASNGKTIEVNNTDAEGRLTLADALVFAEKLEVDAIVDLATLTGACIIALGDNISGLWSTDQTLADQLKAAAETAGEKFWQMPLEEKYFEGLKSPIADMKNTGPRAGGSITAALFLKQFIKDTPWAHLDIAGPVWAEKENGLNNVGGTGFPVRTLVNWVLSF
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
B7K4A4
A1JRL1
SYD_YERE8
Aspartyl-tRNA synthetase
Yersinia
MRTEYCGQLNLSHVGQEVTLCGWVNRRRDLGGLIFIDMRDREGIVQVFFDPDHKAAYEQASELRNEFCIQITGTVRARPDSQINKDMSTGEVEIFANTLNIINRSEPLPLDSNQTNSEEQRLKYRYLDLRRPEMADRLKTRAKITSFVRRFMDSHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTADQVREVMEKLVRELWQETKGVDLGDFPVMTFAEAMRRYGSDKPDLRNPMELVDVADLVKDVEFKVFSGPANDAKGRVAALRVPGGAQVTRKQIDEYGQFVGIYGAKGLAWLKVNDRAAGVEGVQSPIAKFLSAEVLEAILARTQAESGDILFFGADSFKVVTDAMGALRLKVGRDLALTKLDSWAPLWVVDFPMFEDDSEGGLSAMHHPFTAPKDMSPEQLAAAPTTAIANAYDMVINGYEVGGGSVRIHRTEMQQQVFGILGINEEEQREKFGFLLDALKFGTPPHAGLAFGLDRLVMLLTGTDNIRDVIAFPKTTAAACLMTDAPSFANPASLQELSISVVAKKGATDSSVEENQ
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
A1JRL1
Q9SVG0
AVT3C_ARATH
Aromatic and neutral amino acid transporter-like protein 2
Arabidopsis
MGFQNEASSSSYTLKIPPPAREDSPLLGKGPPLSSQFKTFANVFIAVVGAGVLGLPYAFKRTGWLMGVLLLVSVSVLTHHCMMLLVYTRRKLDSFNAGISKIGSFGDLGFAVCGSLGRIVVDLFIILSQAGFCVGYLIFIGTTLANLSDPESPTSLRHQFTRLGSEFLGVSSKSLYIWGCFPFQLGLNSIKTLTHLAPLSIFADIVDLGAMAVVIVEDSMIILKQRPDVVAFGGMSLFLYGMGVAVYSFEGVGMVLPLESEMKDKDKFGKVLALGMGFISLIYIAFGILGYLAFGEDTMDIITANLGAGLVSTVVQLGLCINLFFTFPLMMNPVFEIVERRFSRGMYSAWLRWVLVLAVTLVALFVPNFADFLSLVGSSTCCVLGFVLPALFHLLVFKEEMGWLQWSSDTAIVVLGVVLAVSGTWSSLSEIFSVKV
Translocates preferentially neutral amino acids from the vacuole to the cytoplasm.
Q9SVG0
Q9N1A7
STP2_PANTR
Nuclear transition protein 2
Pan
MDTKTHSLPITHTQLHSNSQPQSCTCTRHRQTFSQSCRQSHCGSRSRSSSQSPASHRNPTGAHSSSGHQSQSPNTSPPPKRHKKTMNSHHSPMRPTILHCSCPKNRKNLEGKLKTKKMAKRIQQVYKTKTRSS
Plays a key role in the replacement of histones to protamine in the elongating spermatids of mammals. In condensing spermatids, loaded onto the nucleosomes, where it promotes the recruitment and processing of protamines, which are responsible for histone eviction.
Q9N1A7
A2QHE5
FDC1_ASPNC
Phenacrylate decarboxylase
Aspergillus subgen. Circumdati
MSAQPAHLCFRSFVEALKVDNDLVEINTPIDPNLEAAAITRRVCETNDKAPLFNNLIGMKNGLFRILGAPGSLRKSSADRYGRLARHLALPPTASMREILDKMLSASDMPPIPPTIVPTGPCKENSLDDSEFDLTELPVPLIHKSDGGKYIQTYGMHIVQSPDGTWTNWSIARAMVHDKNHLTGLVIPPQHIWQIHQMWKKEGRSDVPWALAFGVPPAAIMASSMPIPDGVTEAGYVGAMTGSSLELVKCDTNDLYVPATSEIVLEGTLSISETGPEGPFGEMHGYIFPGDTHLGAKYKVNRITYRNNAIMPMSSCGRLTDETHTMIGSLAAAEIRKLCQQNDLPITDAFAPFESQVTWVALRVDTEKLRAMKTTSEGFRKRVGDVVFNHKAGYTIHRLVLVGDDIDVYEGKDVLWAFSTRCRPGMDETLFEDVRGFPLIPYMGHGNGPAHRGGKVVSDALMPTEYTTGRNWEAADFNQSYPEDLKQKVLDNWTKMGFSN
Catalyzes the reversible decarboxylation of aromatic carboxylic acids like ferulic acid, p-coumaric acid or cinnamic acid, producing the corresponding vinyl derivatives 4-vinylphenol, 4-vinylguaiacol, and styrene, respectively, which play the role of aroma metabolites.
A2QHE5
P17565
Y35K_HALSI
Uncharacterized 36 kDa protein
Halobacterium
MAKRDGMKLRDELTFDTSRAVKAVSWGEAIDRFQSWYDDQRGTQIVVENELGETVGFDMPNRFTPEYREMLYAKAQSLERGLRERWGSLLHTGMVTLTASSTDDEGRLRPPLEHFEDLLESWEAVRRALARVLEGREWEYLAILEPHESGYVHIHLGVFVRGPVVAEQFEPVLDAHLRNCPTAGEDAHQVFDENGDEDAVRVRRSSHPSRSGGVENLGAYLAAYMAGEYGSEPSEMPENVRAFYATMWASGRQWFRPSNGAQELMQPEEDDEGDSIEEWEMVGIAPEGDLGDIIEVDPSEPRSDPYRRLRTPPPGG
Possibly necessary for replication.
P17565
D3ZW55
ITPA_RAT
Nucleoside-triphosphate pyrophosphatase
Rattus
MAASLVGKKIVFVTGNAKKLEEVIQILGDKFPCTLVAQKIDLPEYQGEPDEISIQKCQEAARQVQGPVLVEDTCLCFNALGGLPGPYIKWFLQKLKPEGLYQLLAGFEDKSAYALCTFALSTGDPSQPVLLFRGKTPGQIVMPRGSRDFGWDPCFQPDGYEQTYAEMPKAEKNTISHRFRALFKLQEYFGVTDGAGDH
Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triphosphate (dHAPTP) and xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.
D3ZW55
Q66E18
MTNC_YERPS
2,3-diketo-5-methylthio-1-phosphopentane phosphatase
Yersinia
MIQAIVTDIEGTTTDIRFVHQVLFPYARERLTPFLRAHQQDDDITALLVDLRREIAQPDADIETLITVLHGFMDEDRKSTVLKAIQGIIWRTGYLQADFRGHVYPEVAQQLADWHQQGLKLYVYSSGSVAAQKLLFGYSDAGDLCPLFSGYFDTHVGAKRDVSAYQKIANQLGIAPQALLFLSDIRQELDAAQLAGWHTCQLIRDLPDNDSAHPQVNRFDQIVLSLFTE
Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Q66E18
Q5KC16
RU1C_CRYNJ
U1 small nuclear ribonucleoprotein C
Cryptococcus neoformans species complex
MGKYYCDYCDIYLTHDSMNARKAHNSGRNHVANVRDYFAGLGGNQAQSLIDQIIQQHESGGRNQMMMAPSMRLGAGFMNPLATQPGYPGPPPPGAFPTFPPTAGTPPFRPPFPPSSAPGAPPPTMPPFLPPNASAGAAPGIGMGSTPPFPPNTASPNPGMPPFRPPMGMGMPPAPAQAQAQGSPMGMPQQGQQGTFTPTQEVPQGAGAGIHPDRLRMLGQ
Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. U1-C is directly involved in initial 5' splice-site recognition for both constitutive and regulated alternative splicing. The interaction with the 5' splice-site seems to precede base-pairing between the pre-mRNA and the U1 snRNA. Stimulates commitment or early (E) complex formation by stabilizing the base pairing of the 5' end of the U1 snRNA and the 5' splice-site region.
Q5KC16
Q28U77
MDH_JANSC
Malate dehydrogenase
unclassified Jannaschia
MARPKIALIGAGQIGGTLAHLAALKELGDVVLFDIAEGVPQGKALDIAESGPSEKFDADMSGTNDYADIAGADVCIVTAGVARKPGMSRDDLLGINLKVMKSVGEGIRDNAPDAFVICITNPLDAMVWALREFSGLPHHKVCGMAGVLDSARFRHFLADEFNVSMKDVTAFVLGGHGDTMVPLTRYSTVAGIPLPDLIEMGWTTQEKMDAIVQRTRDGGAEIVGLLKTGSAFYAPATSAIEMAEAYLKDQKRVLPCAAYVDGALGLKGMYVGVPTVIGAGGVERVVDINMTKDEQAMFDNSVAAVNGLVEACKAIDETLS
Catalyzes the reversible oxidation of malate to oxaloacetate.
Q28U77
A8GAC8
DPO4_SERP5
DNA polymerase IV
Serratia
MRKIIHVDMDCFFAAVEMRDDPSLRDIPLAIGGSADRRGVISTANYPARRYGVHSAMSTAMALKLCPHLKLLPGRMAAYKEASQHIREIFARYTPLIEPLSLDEAYLDVTDCSQCNGSATLIAEQIRQTISDELNLTASAGIAPIKFLAKIASELNKPNGQYVITPAQVPAFLQQLPLSKIPGVGKVTAKRLEEVGLITCADVQQYDLAALLKRFGKFGRVLWERCQGIDLREVSPERLRKSVGVERTLAEDIHDWEDCEALIVDKLYPELELRLRKVKPDLHIARQGVKLKFQDFQQTTQEHVWPVLNKDDLINVARQVWRERREGRGVRLVGLHVTLLDPQLERQLLLPWE
Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
A8GAC8
P0A3X9
CYC6_THEVB
Soluble cytochrome f
Thermosynechococcus
MKKRFISVCAIAIALLVSLTPAALAADLANGAKVFSGNCAACHMGGGNVVMANKTLKKEALEQFGMYSEDAIIYQVQHGKNAMPAFAGRLTDEQIQDVAAYVLDQAAKGWAG
Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis.
P0A3X9
B0KCK4
RS19_THEP3
30S ribosomal protein S19
Thermoanaerobacter
MSRSVKKGPYVDPKLLKKIVEMNKKNEKKVIKTWSRSSTIVPEMVGHTIAVHDGRKHVPVYITEAMVGHKLGEFAPTRTFHGHADTEKTSKVK
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
B0KCK4
Q8NFZ0
FBH1_HUMAN
F-box only protein 18
Homo
MRRFKRKHLTAIDCQHLARSHLAVTQPFGQRWTNRDPNHGLYPKPRTKRGSRGQGSQRCIPEFFLAGKQPCTNDMAKSNSVGQDSCQDSEGDMIFPAESSCALPQEGSAGPGSPGSAPPSRKRSWSSEEESNQATGTSRWDGVSKKAPRHHLSVPCTRPREARQEAEDSTSRLSAESGETDQDAGDVGPDPIPDSYYGLLGTLPCQEALSHICSLPSEVLRHVFAFLPVEDLYWNLSLVCHLWREIISDPLFIPWKKLYHRYLMNEEQAVSKVDGILSNCGIEKESDLCVLNLIRYTATTKCSPSVDPERVLWSLRDHPLLPEAEACVRQHLPDLYAAAGGVNIWALVAAVVLLSSSVNDIQRLLFCLRRPSSTVTMPDVTETLYCIAVLLYAMREKGINISNRIHYNIFYCLYLQENSCTQATKVKEEPSVWPGKKTIQLTHEQQLILNHKMEPLQVVKIMAFAGTGKTSTLVKYAEKWSQSRFLYVTFNKSIAKQAERVFPSNVICKTFHSMAYGHIGRKYQSKKKLNLFKLTPFMVNSVLAEGKGGFIRAKLVCKTLENFFASADEELTIDHVPIWCKNSQGQRVMVEQSEKLNGVLEASRLWDNMRKLGECTEEAHQMTHDGYLKLWQLSKPSLASFDAIFVDEAQDCTPAIMNIVLSQPCGKIFVGDPHQQIYTFRGAVNALFTVPHTHVFYLTQSFRFGVEIAYVGATILDVCKRVRKKTLVGGNHQSGIRGDAKGQVALLSRTNANVFDEAVRVTEGEFPSRIHLIGGIKSFGLDRIIDIWILLQPEEERRKQNLVIKDKFIRRWVHKEGFSGFKRYVTAAEDKELEAKIAVVEKYNIRIPELVQRIEKCHIEDLDFAEYILGTVHKAKGLEFDTVHVLDDFVKVPCARHNLPQLPHFRVESFSEDEWNLLYVAVTRAKKRLIMTKSLENILTLAGEYFLQAELTSNVLKTGVVRCCVGQCNNAIPVDTVLTMKKLPITYSNRKENKGGYLCHSCAEQRIGPLAFLTASPEQVRAMERTVENIVLPRHEALLFLVF
3'-5' DNA helicase and substrate-recognition component of the SCF(FBH1) E3 ubiquitin ligase complex that plays a key role in response to stalled/damaged replication forks . Involved in genome maintenance by acting as an anti-recombinogenic helicase and preventing extensive strand exchange during homologous recombination: promotes RAD51 filament dissolution from stalled forks, thereby inhibiting homologous recombination and preventing excessive recombination . Also promotes cell death and DNA double-strand breakage in response to replication stress: together with MUS81, promotes the endonucleolytic DNA cleavage following prolonged replication stress via its helicase activity, possibly to eliminate cells with excessive replication stress . Plays a major role in remodeling of stalled DNA forks by catalyzing fork regression, in which the fork reverses and the two nascent DNA strands anneal . In addition to the helicase activity, also acts as the substrate-recognition component of the SCF(FBH1) E3 ubiquitin ligase complex, a complex that mediates ubiquitination of RAD51, leading to regulate RAD51 subcellular location .
Q8NFZ0
B2RZR0
DDL_BORHD
D-alanylalanine synthetase
Borrelia
MMKKNLMLIFGGVSFEHEISLRSAYGIYSALMKLDKYNLYPSFIDKITGIWYLLDSVPDAPELIKRDSSAIISLIPGCGIFVNDEDLEIDVVFPIVHGRTGEDGAIQGFLKMMDIPCVGAGILGSAISINKYFCKLLLKSFNIPLVPFIGFRKYDYFLDKEGIKKDIKQSLNYPVIVKPAMLGSSIGISIAYNDTQIEKCIEEAFEYDLTVVVEKFMKVREIECSVIGNEQIKIFTPGEIVVQDFVFYDYDAKYSTIPGNSVVFNIPARLDMKHLLDIKEYAFLTYKCLELRGMARIDFLIEKDTNLIYVNEINTIPGFTDISMFSKMCEHDGLDYESLVDNLVSLAFQSYAKRKERIDFKRLEN
Cell wall formation.
B2RZR0
Q85G35
SECA_CYAM1
Protein translocase subunit SecA
Cyanidioschyzon
MKNKLRQIKENREKYRKLKEEELREKTKQLKERAKQESLEELMVEAYSNVWEGAARVLKLEAYDVQLIGAMVLNKGQIAEMKTGEGKSLVAAFASYLNALSGKGVHIVTVNDYLAKRDERWIGEVLRYLGLKTAVITNESSREERKKGYEADVTYITNSELGFDYLRDHMAWSKEEIVQREFNYCIIDEVDSILIDEARTPLIISGPTKGSEKPYKVAWEIGKRMKEGEDYELEEKSKQVILKEKGIKRCEEALEVKDIFSMETPWAHYVMNAIKAKHFYIKDVNYIIKEGEVVIVDEFTGRIMGGRRWADGLHQAIEAKEGVKIQEESETLASITYQNLFLLYPKLAGMTGTAKTEEEEFEQIYGLKVVSIPTHRKMKRKDYPDVVYRTSRSKWMAVAEECERMWTKGRPVLVGTTSIEKSELLARLLEEKGVKYKLLNARPSLAADEASIIAQAGKIGSITIATNMAGRGTDIILGGNIKEAFGEWIKERKKQVDIEEEWRKVLEGKADEESEKKYKQLKEEHEKEQKRVKQLGGLYVIGTERHESRRIDNQLRGRSGRQGDEGSSRFFISLEDDLLRIFGGGQMGEIMSRLGVEEPLESAFLSKSLDRAQKKVENYYYQMRKQLFEYDQVLNSQRKAIYKERTDILRSEEVGEWSKSYIRKEWPGGLLGIKRGMRNRSEVEISYDVKKMQMESVQAGLMNELERLLLLQQIDKSWSKHLKEMSLLREFIAWRGYAQRDPLVEYKNESYNLFIKMIEEIRQGYAYSLFRSQA
Has a central role in coupling the hydrolysis of ATP to the transfer of proteins across the thylakoid membrane.
Q85G35
Q9I927
FUCL5_ANGJA
Fucolectin-5
Anguilla
MKTCNLTDRMKVKMIMLLFQILAISTLQSDSAYIPDRYTQENVAVRGKATQSALASGGGAVLSLPGYAIDGNRDSDSSHGSCSHTTNGPNPWWRVDLLQVYTIASVTITNRGDCCGERITGAHILIGNSLENNGINNPQCSTVGIMTAGETRTFHCSRPMIGRYVTVYLPKTEYLQLCEVEVNALLPAN
Acts as a defensive agent. Recognizes blood group fucosylated oligosaccharides including A, B, H and Lewis B-type antigens. Does not recognize Lewis A antigen and has low affinity for monovalent haptens.
Q9I927
P0C8X9
KAXU2_HOFGE
Potassium channel toxin alpha-KTx
Hadrurus
MKNIAMKTTVVLTILLLSVLTAINADTMKKRSDYCSNDFCFFSCRRDRCARGDCENGKCVCKNCHLN
Blocks Kv1.1/KCNA1, Kv1.2/KCNA2 and Kv1.3/KCNA3 voltage-gated potassium channels.
P0C8X9
Q57QM5
NANM_SALCH
Sialic acid epimerase
Salmonella
MGMQMKNFKKMMTLMALCLSVAITTSGYATTLPDIPEPLKNGTGAIDNNGVIYVGLGTAGTSWYKIDLKKQHKDWERIKSFPGGAREQSVSVFLNDELYVFGGVGKKNSESPLQVYSDVYKYSPVKNTWQKVDTISPVGLTGHTGVKLNETMVLITGGVNEHIFDKYFIDIAAAAADESEKNKVIYNYFNKPAKDYFFNKIVFIYNAKENTWKNAGELPDAGTAGSSSVMENNFLMLINGELKPGLRTDVIYRAMWDNDKLTWLKNSQLPPSPGEQQQEGLAGAFSGYSHGVLLVGGGANFPGAKQNYTNGKFYSHEGINKKWRDEVYGLVNGHWQYMGKMKQPLGYGVSVSYGDEVFLIGGENAKGKPVSSVTSFTMRDGNLLIK
Converts alpha-N-acetylneuranimic acid (Neu5Ac) to the beta-anomer, accelerating the equilibrium between the alpha- and beta-anomers. Probably facilitates sialidase-negative bacteria to compete sucessfully for limited amounts of extracellular Neu5Ac, which is likely taken up in the beta-anomer. In addition, the rapid removal of sialic acid from solution might be advantageous to the bacterium to damp down host responses.
Q57QM5
A8EYM5
CLPP_RICCK
Endopeptidase Clp
belli group
MSYVPIVIEQTSRGERAYDIYSRLLKERIIFVCSTVEDHMANLIVAQLLFLEAENPKKDIYMYINSPGGVVTAGLAIYDTMQYIKPKVATLCIGQACSMGSFLLCGGEKGMRYSLPHSRIMIHQPSGGYQGQATDIEIHAQETLKIKRLLNELYSKHTGQDVKHIEKSMERDNFMSPEEAKKFGIVDNIISSRNATGLLTK
Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
A8EYM5
P0CH47
PA1_VESMG
Probable phospholipase A1 magnifin
Vespa
MNLKYLLLFFCLVQVLHYCYSHGDPSLSNELDRGLIPKCKLVPEQISFVLSTRENQNGVFLTLDNLSKGGILPKSDLSSIPVIFLIHGFISSANNSNYVDMTKALLEKNDCMVISIDWRDGACTHEFKILKFIGYPNAVKNTRAVGKYIADFTKLLMQKYKVSLANIRLIGHSLGAQIAGFAGKEYQKFKLGKYPEIIGLDPAGPLFKSNDCSERICETDAHYVQIIHTSNNLGTERTLGTVDFYVNNGYNQPGCYLSFLGEACSHTRAVKYFTECIRHECCLIGVPQSKNPQPVSKCTRKECVCIGLNAKTYPKTGSFYVPVESKAPYCNNKGKKI
Has phospholipase activity, probably a phospholipase A1 activity as suggested by sequence similarity. In vivo, induces dose-dependently platelet aggregation at nanomolar concentration and induces thrombosis in vivo .
P0CH47
Q6MF52
AROB_PARUW
3-dehydroquinate synthase
Candidatus Protochlamydia
MLNSSNYVIQSHCLDDLKYYLESLSYSKVVIITHPQLWVMYEQKITEQLFKLSWNFSVLLIPEGETSKSLKQTTRCWRHFIKHQLDRYSLVVALGGGVICDLAGFVASCYMRGIDTIYLPTTLLAMVDASIGGKTGINTSKSKNIIGSFHLPKKILIDPFTLKTLSKKHYQAGFAEIIKYGMIASPSLFEFLENSWSLIEQRDEGLLEIIIQQSCAIKKKYVEADFKDLGIRAQLNYGHTFGHVIEMMSRYQYLHGEAVSIGMSCAAYLSCQMGLTTQETMQRQDALCQQAQLPIHLPHFPLTRFTYLMAKDKKGRNGSINLILPEKVGKVTQIFDVDPHLIKNTLSTKMTK
Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
Q6MF52
Q7CI09
EFEB_YERPE
Peroxidase EfeB
Yersinia
MRDKTGPKFGPYQPDDEAVSPSRRRLILGMGMVSGALVLGGAKTAQAADCRSPDVAGTQDERWQKQPFYGQHQAGVLTPQQAAMMLVAFDVLATDKTSLIRLFKLLTERLAFLTTGGRAPSVNAKLPPLDSGIMGPEIYPDNLTVTVSVGNALFDERFGLQGQKPLRLQRMTRFPNDSLDAGLCHGDVMLQICANTNETVIHALRDIIKHTPDLLSVRWKREGFISAHAARSKGQDTPINLLGFKDGTANPKISNKPLINNVVWVSNNAGEPAWAVGGSYQVVRIIRFKVEFWDRTPLQEQQTIFGRDKNSGAPLGMQHEHDEPNYAKDPEGKVIPMDAHIRLANPRTIETQRNLMLRRGYSYSLGVSNSGQLDMGLLFVCYQSDLAQAFLTVQERLNGEALEEYVKPIGGGYFFTLPGVADANHYLAQSLLEA
Involved in the recovery of exogenous heme iron. Extracts iron from heme while preserving the protoporphyrin ring intact.
Q7CI09
Q5SD39
CYF_HUPLU
Cytochrome f
Huperzia
MQNVNTYDCIKKLVTQLISVLIVINTIAWPSIPKAYPIFAQQSYENPREATGRIVCSNCHLAKKLVDIEVPQSVLPNTVFEAVVKIPYDMQIKQVLANGKKGALNVGAVLILPEGFELAPPDRIPPDTKEKIGNLYFQAYRPNKNNILVIGPVPGKKYSEIVFPILSPDPALNKETHFLKYPIYVGGNRGRGQIYPDGSKSNNTVYNASATGRVSKISRKEKGGYEITVENTLDGRSVVDTVPPGPELIISEGESIKVDQPLTNNPNVGGFGQGDAEVVPQDPLRVQGLLLFLASVTIAQIFLVLKKKQFEKVQLAEMNF
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Q5SD39
O42933
PMT4_SCHPO
Dolichyl-phosphate-mannose--protein mannosyltransferase 4
Schizosaccharomyces
MASKSEKAVKKAQKLSKEPSVELTDTKSSDNVTPKQKSPNSTEEDVSLNLKTLKAKKFKLAFVLITVLSFITRFWNLNLPGEVVFDEVHFGKFASYYLQGKYFFDLHPPFAKLLLALVAKLAGYDGHYLFDNIGDNYKDNGVPYVTIRAWPALLSSLVPPVVFLIMKESGYDLLACIVSSSLVLFDNAHVTEGRLILLDATLLFSMVCAIYCYVRFFKLRHTPFSRPWWAWLFFTGFFLSCTISTKYVGFFTFLSIGLSVCLELWYLWDIKTGLTVERFFQHFLARFFCLIFFPFLFFLFWFYMHFNILTISGPGDSFMSLEFQETLSDNPITANSTILNYYDIVTIKHMGTNAFLHSHPEKYPIPYDDGRISSGGQQVTGYQFDDENNYWMILPADHYDPPIEAKLNVPVKNMDYIKLHHVGTNTDLMTHDVASPYHPTNEEFTTVSVDESAGKKHEYTLFQVVMSDNTDPQRPLYTKASSFKLIHKLTHVAMWSDPKPLPDWAFKQLEINGAKNIQTGSIFWTFDDIIGLKDSRLKKEKKIPKKLPFWKKYLELQLTMFRQNNMLTEFHPYSSNPSDWFTLHHGIAFWAKSEENKQIYLLGNPIGWWIIAGTVLSTTVVAAAEILLRQRGIRTLPETVRNHFYRSTMFFYMTYVFHYLPFFIMGRQLFLHHYLPAHLAGSLLVGAFIQLACRKSFRSPVSAGVPIPKDVDEKGHSKCHRKYGHVIELICTLLLIFVVIYCFTFFAPMTYGDKSLSVDEWTRRKWLDSWVFQYQKQN
Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. Required for normal cell wall and septum formation.
O42933
Q8TXB5
RF1_METKA
Translation termination factor aRF1
Methanopyrus
MAESSTVERYRFRKMIERLENLRGQGTELITIYIPPENRLSDVIAQMREEYSQASNIKSKRTRKNVQSAIEVVMQRLKMVGETPENGLVVLVGTVQDGTKEKMVAELIEPPEPVDRFIYRCDSKFYLEPLKEYLEEKDVYGILVMDRREATIGLVKGKRIEPVKRLTSDVPGKHKAGGQSQRRFDRLIEHAAHEFYQKVGEAAREAFEDVKDLKGIIVGGPGPTKEEFLDGDYLPKDLKEKVLTVVDVGNTDESGLREALNKAEEALKEAELVREKRLVRKFMEEAVNGELAAYGEEVDELLKMGAVEVLLVSEDLEGYKVILRCPECGYENIVTVKEKDEAKKYVEECPECGEAELNVEEIKDIVDYYVELAEQMGSNVEIISTETEEGAQFYNAFRGLGALLRFRPK
Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA.
Q8TXB5
A6ZX66
AQY1_YEAS7
Aquaporin-1
Saccharomyces
MSSNDSNDTDKQHTRLDPTGVDDAYIPPEQPETKHHRFKISKDTLRNHFIAAAGEFCGTFMFLWCAYVICNVANHDVALVAAPDGSHPGQLIMIAIGFGFSVMFSIWCFAGVSGGALNPAMSLSLCLARAVSPTRCVVMWVSQIVAGMAAGGAASAMTPGEVLFANSLGLGCSRTRGLFLEMFGTAILCLTVLMTAVEKRETNFMAALPIGISLFIAHVALTAYTGTGVNPARSLGAAVAARYFPHYHWIYWIGTLLGSILAWSVWQLLQILDYTTYVTAEKAASTKEKAQKKGETSSSSAVAEV
Water channel required to facilitate the transport of water across membranes. Involved in sporulation, freeze tolerance and osmotolerance. Is non-functional in most laboratory strains.
A6ZX66
Q48F77
PYRG_PSE14
UTP--ammonia ligase
Pseudomonas
MTRYIFVTGGVVSSLGKGIASASLAAILEARGLKVTMLKLDPYINVDPGTMSPFQHGEVFVTHDGAETDLDLGHYERFIRTTMTQNNNFTTGRVYEHVLRKERRGDYLGATIQVIPHITDEIKRRIIKGAGDADVALVEIGGTVGDIESQPFLEAIRQLRFEVGARRAMLMHLTLVPYIATAGETKTKPTQHSVKELRSIGLQPDVLVCRSDHPIDVSSRRKIAQFTNVEERAVIALEDADTIYKIPGILHSQGLDDFVVERFGLQCEGADLSEWDKVVDAKLNPEHEVTIAMVGKYMELLDAYKSLIEAMSHAGITNRTKVNLRYIDSEDIENQGTGLLEGVDAILVPGGFGLRGVEGKITAVQFARENKVPYLGICLGMQVAVIEFARNVLGWKDANSTEFNRTSAHAVVGLITEWEDATGAVETRTESSDLGGTMRLGAQDCQLEAGSLVHDCYRKDVIVERHRHRYEVNNNLLPQLIEAGLKISGRSGDGALVEVVEAPDHPWFVACQFHPEFTSTPRDGHPLFSGFVKAALAQHQKNS
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
Q48F77
Q07KM4
RS3_RHOP5
30S ribosomal protein S3
Rhodopseudomonas
MGQKINPIGLRLGINRTWDSRWFAGKNEYGKLLHEDVKIRAILHKELKQAAVARIVIERPHKKCRVTIHSARPGVVIGKKGADIDKLRKKVADITASDVVINIVEIRKPELDATLVAESIAQQLERRVAFRRAMKRAVQSAMRLGAEGIRINCSGRLGGAEIARMEWYREGRVPLHTLRADIDYGVATAFTTFGTCGVKVWIFKGEILEHDPMAQDKRMAEGDNSRPRRDAA
Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.
Q07KM4
B0UJ78
PURA_METS4
IMP--aspartate ligase
Methylobacterium
MANVVVVGAQWGDEGKGKIVDWLAEQADVVVRFQGGHNAGHTLVIDGVTYKLSLLPSGVVRGGTLSVIGNGVVVDPWHLVDEIARIGTQGVSITPETLRIADNATLILPLHRELDHFRETANATLKIGTTKRGIGPAYEDKVGRRAIRVVDLADEALLGAKIERLLAHHNALRRGLGIEEVDGAALKAELLAIAPKILPYADTVWVLLDEARRGGQRILFEGAQGALLDVDHGTYPYVTSSNIVAAQAATGSGLGPSAIGYVLGIVKAYTTRVGEGPFPTELTDAIGEKIGERGREFGVVTGRKRRCGWFDAALVRQTVRTSGIDGIALTKLDILDGFETIKICTGYRLDGRLIDHLPASQADQARVEPVYETIDGWFETTAGARSWAELPAQAIKYVRRIEELIGATVALLSTSPERDDTILVHNPFED
Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
B0UJ78
Q5F5Y7
DAPB_NEIG1
4-hydroxy-tetrahydrodipicolinate reductase
Neisseria
MIPLKIAIAGANGRMGRVLVEAVNNHPDTVLSGALEHSGSEALGLDAGYAVGLKTGIAISDDVDAVLAQSDVLIDFTRPEPTLKHLQKCVEKQVNIIIGTTGFDDAGKAAIRAAAEKTGIVFAANFSVGVNLTFHILDTVARVLNEGYDIEIIEGHHRHKVDAPSGTALRMGEVIAGALGRDLKQCAVYGREGHTGPRDPSTIGFATVRAGDIVGDHTALFATDGERVEITHKAGSRMTFAAGAVRAAVWVNGKTGLYDMQDVLGLNNR
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
Q5F5Y7
Q5WB73
ATPL_ALKCK
Lipid-binding protein
Alkalihalobacillus
MTELAIGIAAGLAAIGGAIGVAIIVKAVIEGTARQPEQRGTLQTLMFIGAPLAEAVPIIAIVIAFLLFFMG
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.
Q5WB73
B0KF32
TSAC_PSEPG
tRNA threonylcarbamoyladenosine biosynthesis protein TsaC
Pseudomonas
MVSSFRVQQAAREIRAGAVIAYPTEAVWGLGCDPWNEDAVYRLLALKSRPVDKGLILIADNIRQFDFLFEDFPEDWIERMGSTWPGPNTWLVPHQDLLPEWVTGKHDTVALRVTDHPQVRELCALVGPLISTSCNPGGRPAAKTRLRVEQYFHGQLDLVLGGALGGRKNPSVIRNLATGEVVRPG
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate.
B0KF32
P47983
ZP2_CANLF
Processed zona pellucida sperm-binding protein 2
Canis
MACKQKGDSGSPSSRFSADWSTYRSLSLFFILVTSVNSVGVMQLVNPIFPGTVICHENKMTVEFPRDLGTKKWHASVVDPFSFELLNCTSILDPEKLTLKAPYETCSRRVLGQHQMAIRLTDNNAASRHKAFMYQISCPVMQTEETHEHAGSTICTKDSMSFTFNIIPGMADENTNPSGGKWMMEVDDAKAQNLTLREALMQGYNFLFDSHRLSVQVSFNATGVTHYMQGNSHLYTVPLKLIHTSPGQKIILTTRVLCMSDPVTCNATHMTLTIPEFPGKLQSVRFENTNFRVSQLHNHGIDKEELNGLRLHFSKSLLKMNSSEKCLLYQFYLASLKLTFAFERDTVSTVVYPECVCEPPVTIVTGDLCTQDGFMDVKVYSHQTKPALNLDTLRVGDSSCQPTFKAPSQGLTLFHIPLNGCGTRLKFKGDTVIYENEIHALWTDLPPSTISRDSEFRMTVKCHYSRDDLLINTNVQSLPPPVASVRPGPLALILQTYPDKSYLRPYGDKEYPVVRYLRQPIYLEVKVLNRADPNIKLVLDDCWATPTMDPASLPQWNIVMDGCEYNLDNYRTTFHPVGSSVTYPTHYQRFDVKTFAFISEAQVLSSLVYFHCTALICNRLSPDSPLCSVTCPVSSRHRRATGSTEEEKMIVSLPGPILLLADSSSLRDGVDSKGHRAAGYVAFKTVVAVAALAGLVAALGLIIYLRKKRTMVLNH
Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP2 may act as a secondary sperm receptor.
P47983
C1CEB0
GLGA_STRZJ
Starch [bacterial glycogen] synthase
Streptococcus
MKILFVAAEGAPFSKTGGLGDVIGALPKSLVKAGHEVAVILPYYDMVEAKFGNQIEDVLHFEVSVGWRRQYCGIKKTVLNGVTFYFIDNQYYFFRGHVYGDFDDGERFAFFQLAAIEAMERIDFIPDLLHVHDYHTAMIPFLLKEKYCWIQAYEDIETVLTIHNLEFQGQFSEGMLGDLFGVGLERYADGTLRWNNCLNWMKAGILYANRVSTVSPSYAHEIMTSQFGCNLDQILKMESGKVSGIVNGIDADLYNPQTDALLDYHFNQEDLSGKAKNKAKLQERVGLPVRADVPLVGIVSRLTRQKGFDVVVESLHHILQEDVQIVLLGTGDPAFEGAFSWFAQIYPDKLSANITFDVKLAQEIYAACDLFLMPSRFEPCGLSQMMAMRYGTLPLVHEVGGLRDTVRAFNPIEGSGTGFSFDNLSPYWLNWTFQTALDLYRNHPDIWRNLQKQAMESDFSWDTACKSYLDLYHSLVN
Synthesizes alpha-1,4-glucan chains using ADP-glucose.
C1CEB0
C5C0V6
EX7S_BEUC1
Exodeoxyribonuclease VII small subunit
Beutenbergia
MSQEPPARPDPATLSYEQARAELVDVVQRLEQGAATLEDSLALWERGEALAARCQEWLDGARDRLARVSPASGGATEAPAPAERDR
Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
C5C0V6
Q75CM4
SBE2_ASHGO
Protein SBE2
Eremothecium
MEVPADSSSCLQVKRVHSLSVLKNKVSCFFLTIYWANALSRDSARVAGLDSEVRVRRDCELREGGMPSVLGTLDESMAEDAFGLGVDGYSEGASMFTADVTRLGRPLRRRAAGGDAGRAGEGAGAAGGLGRGGEARGGAAEAAETAEALDFQPPPSKLFAGRVERPISNDSIVTEAAETLSTHFDMSASTSSSSRGSSVVIEKSQAHEAAEESATGAPCKKYLFASSRDRLQLSLGGMEASLSSLHIPAAGADAGGAVHSVASFSRTAPALVTTSKALTPSQRYRLRREQNKVALQNSIKQREVFYEEQERGSRGRSASLKGVLGLPHAVDELSEDISDYLGWDVPVVSPTTGPFLAAAERSEKHTDRRPGVARSRSSTYVDHTMPPSPIPGIQKTSDLEFFTETSKKLSCVYLDTSKETSKSKLYERSQSAELLPIEFKAASDEGMEDLKLVSSGKMAVCSNSRPSWLPPKDTEERARHERQIRQTIDIASLSQIDRTKERAERDTRDEKNRKRLAQLVERGLVRKSTLTELKKICWETSLPPDSRFQIYTTLLQSDTAKLIEEQYIDNFDQVDALFRSMQFPNAKLAEIQAMLACTPCTANVAPADDLIYLLQLKAISRQGLLLGDPLLVHHLLQVGCYSTREIWVLVNILQLTCFNETTKDKYDRRIISSRGTVSTALSADKTFAQEFNSKCLNFTTWWHLMARLDHAVFMWCLDIIVAENSQPFKSNPIIRDKLNGKDWDYYRDLHVVVNYRIICALTLTVLLSYHFGFNNLYDLSFVDPAFQIIGPEQGDLGDVHATFIKKWHHNYKKF
With SBE22, is involved in cell wall integrity and polarity processes like bud growth.
Q75CM4
Q7ZWX9
MIDNB_XENLA
Midbrain nucleolar protein B
Xenopus
MEQQPSVPRSCTNVARETPMNLNIQSTTGTRYELSVPLNETVDGLKRRISQRLKVPKERLTLLHRETRLSSGKLQDLGISDGSRLTLLPSVEAGLMSQMSRPEQSVMQALESLTETQVNDFLSGRSPLTLALRVGDHMMFVQLQLAAQQSGGSHLQHRHVITRGADAGAPPQYRTLHTSTSALSHLASCTPGSTPPTTLSPTSSTHCDAPHSSPLTTSVFRSHGEGVSPCAEQVPCSTRGTEGTSSSPSSRSRKPGAIIESFVNHAPGVFSGTFSGTLHPHCQDGAGRPRRDIGTILQILNDLLSATRHYQGMPPSLTTLRCHTQCASQARNAKATSPQSTGPQQTTHPVGHCQAQTRTCKPSGDRLRQTENRATRCKVERLQLLMHQKRLRRKARRDSRAPYHWMPTRKSSRTSSNSSTSSGEGSLEIDFEDSLWKPDVKAELNSEFVVA
Facilitates ubiquitin-independent proteasomal degradation of polycomb protein CBX4. Plays a role in inhibiting the activity of glucokinase GCK and both glucose-induced and basal insulin secretion.
Q7ZWX9
P19538
CI_DROME
ci form of 75 kDa
Sophophora
MDAYALPTYFPLAYSELQFLASRRAAAVAAAATVLPGSPCINQHHPTDVSSSVTVPSIIPTGGTSDSIKTSIQPQICNENTLLGNAGHQHNHQPQHVHNINVTGQPHDFHPAYRIPGYMEQLYSLQRTNSASSFHDPYVNCASAFHLAGLGLGSADFLGSRGLSSLGELHNAAVAAAAAGSLASTDFHFSVDGNRRLGSPRPPGGSIRASISRKRALSSSPYSDSFDINSMIRFSPNSLATIMNGSRGSSAASGSYGHISATALNPMSHVHSTRLQQIQAHLLRASAGLLNPMTPQQVAASGFSIGHMPTSASLRVNDVHPNLSDSHIQITTSPTVTKDVSQVPAAAFSLKNLDDAREKKGPFKDVVPEQPSSTSGGVAQVEADSASSQLSDRCYNNVVNNITGIPGDVKVNSRLDEYINCGSISIPSNEYDCANADTTDIKDEPGDFIETNCHWRSCRIEFITQDELVKHINNDHIQTNKKAFVCRWEDCTRGEKPFKAQYMLVVHMRRHTGEKPHKCTFEGCFKAYSRLENLKTHLRSHTGEKPYTCEYPGCSKAFSNASDRAKHQNRTHSNEKPYICKAPGCTKRYTDPSSLRKHVKTVHGAEFYANKKHKGLPLNDANSRLQQNNSRHNLQEHNIDSSPCSEDSHLGKMLGTSSPSIKSESDISSSNHHLVNGVRASDSLLTYSPDDLAENLNLDDGWNCDDDVDVADLPIVLRAMVNIGNGNASASTIGGSVLARQRFRGRLQTKGINSSTIMLCNIPESNRTFGISELNQRITELKMEPGTDAEIKIPKLPNTTIGGYTEDPLQNQTSFRNTVSNKQGTVSGSIQGQFRRDSQNSTASTYYGSMQSRRSSQSSQVSSIPTMRPNPSCNSTASFYDPISPGCSRRSSQMSNGANCNSFTSTSGLPVLNKESNKSLNACINKPNIGVQGVGIYNSSLPPPPSSHLIATNLKRLQRKDSEYHNFTSGRFSVPSYMHSLHIKNNKPVGENEFDKAIASNARRQTDPVPNINLDPLTNISRFSTTPHSFDINVGKTNNIASSINKDNLRKDLFTVSIKADMAMTSDQHPNERINLDEVEELILPDEMLQYLNLVKDDTNHLEKEHQAVPVGSNVSETIASNHYREQSNIYYTNKQILTPPSNVDIQPNTTKFTVQDKFAMTAVGGSFSQRELSTLAVPNEHGHAKCESFHHQSQKYMNTDIGSKQQSALPSAHQRQTEKSNYNQIIDSSMTSLPELNVDSIYPRNETENIFKVHGDHDNEIQCGIISQSQMSPSTNLNNDGQFSTVNMQPITTSKLFPPEPQKIVCDTQASNTSVMHLDTYQRTLEYVQSCQNWMETNNTSTNQIQSLPGMPVNNTLFPDVSSSTHPYHGTNMVINDMTTSLTSLLEENRYLQMMQ
Has a dual function as a transcriptional activator and a repressor of the hedgehog (Hh) pathway. The full-length ci form (ciFL), acts as an activator (ciA) while ciR, its C-terminally truncated form, acts as a repressor. Involved in segment polarity. Required for the normal development of the posterior half of each embryonic segment. Engrailed protein directly represses ci expression in posterior compartment cells. Essential component of a hh-signaling pathway which regulates the Duox-dependent gut immune response to bacterial uracil; required to activate Cad99C-dependent endosome formation, norpA-dependent Ca2+ mobilization and p38 MAPK, which are essential steps in the Duox-dependent production of reactive oxygen species (ROS) in response to intestinal bacterial infection .
P19538
Q55664
ALF2_SYNY3
Fructose-bisphosphate aldolase class II
unclassified Synechocystis
MALVPMRLLLDHAAENGYGIPAFNVNNMEQIISIMQAADETDSPVILQASRGARSYAGENFLRHLVLGAVETYPHIPIAMHQDHGNSPATCYSAIRNGFTSVMMDGSLEADAKTPASFEYNVNVTAEVVKVAHSVGASVEGELGCLGSLETGQGEAEDGHGFEGKLDHSQLLTDPEEAVEFVNKTQVDALAVAIGTSHGAYKFTRKPTGEVLAISRIEEIHRLLPNTHLVMHGSSSVPQEWIDMINEFGGAIPETYGVPVEEIQKGIKSGVRKVNIDTDNRLAITAAFREAAAKDPKNFDPRHFLKPSIKYMKQVCADRYQQFWTAGNASKIKQLTLDDYAAKYAKGELTATSRTSVAV
Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis.
Q55664
P18550
RR19_PETHY
30S ribosomal protein S19, chloroplastic
Petunia
MTRSLKKNPFVANHLLNKIDKLNT
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
P18550
Q32L79
INSL6_BOVIN
Insulin-like peptide INSL6 A chain
Bos
MPRFLYLCLGLLLVRVSRELNDISRARRLCGQHLLHEIVKLCGDVNWSHVEKEKPFTQLLSQASEKVESFIPDRSESSQTTFPVWRRATNPVPTSASQEEAINNMKMQSLPEYQYKKANLPFKTRQEESSSSQDISPYIHEIIEFQKKNTNKIKTLSNLFWGNHPQRKRRGYSEKCCQKGCTKEELIIACLPYIDYENLRKHQQL
May have a role in sperm development and fertilization.
Q32L79
Q1JC06
LEPA_STRPB
Ribosomal back-translocase LepA
Streptococcus
MNSQDLKKRQEKIRNFSIIAHIDHGKSTLADRILEKTETVSSREMQAQLLDSMDLERERGITIKLNAIELNYTAKDGETYIFHLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNDLEILPVINKIDLPAADPERVRHEVEDVIGLDASEAVLASAKAGIGIEEILEQIVEKVPAPTGDVDAPLQALIFDSVYDAYRGVILQVRIVNGIVKPGDKIQMMSNGKTFDVTEVGIFTPKAVGRDFLATGDVGYVAASIKTVADTRVGDTVTLANNPAKEALHGYKQMNPMVFAGIYPIESNKYNDLREALEKLQLNDASLQFEPETSQALGFGFRCGFLGLLHMDVIQERLEREFNIDLIMTAPSVVYHVHTTDEDMIEVSNPSEFPDPTRVAFIEEPYVKAQIMVPQEFVGAVMELSQRKRGDFVTMDYIDDNRVNVIYQIPLAEIVFDFFDKLKSSTRGYASFDYDMSEYRRSQLVKMDILLNGDKVDALSFIVHKEFAYERGKIIVEKLKKIIPRQQFEVPIQAAIGQKIVARSDIKALRKNVLAKCYGGDVSRKRKLLEKQKAGKKRMKAIGSVEVPQEAFLSVLSMDDRCQEITKPNRLVFRGELLWAYMTKKLIIS
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.
Q1JC06
Q7XRX3
HFB2A_ORYSJ
Heat stress transcription factor 14
Oryza sativa
MASPAAGTPPFLTKTYAMVEDPSTDETISWNDSGTAFVVWRPAEFARDLLPKHFKHSNFSSFVRQLNTYGFKKVVADRWEFANDCFRRGEKHLLGGIQRRKGSGTGGAGAAPAGGIPTAIPISSPPTSSGGEPAVSSSPPRGAAGIAAGVSGAVAELEEENARLRRENARLARELARARRVCDGVRRLVSRYDHDHGGGEEEAGEGDVKPMLFGVAIGGKRSREENGEDEEEEEEEGADEDGEDDEVEEDDEERERHAARRVPVREGKVRRTTELSDLDVLALSVRAAAAARPGGASRDRKSSVS
Transcriptional regulator that specifically binds DNA of heat shock promoter elements (HSE).
Q7XRX3
Q2SL57
RIMM_HAHCH
Ribosome maturation factor RimM
Hahella
MSEKVCIGKIVGVYGVKGWLKVRSFTSPPENMLRYANWELVREDGNRSSAKLRSGKPQGKGIVIALAGVDDRNLAKSYVGCQIEIESSELPALEEGEYYWRQLEGLTVFTSEGVNIGRVSHLIETGANDVLVVIGSAESIDKRERLIPYLPGQFIENIDLDKNLMVVDWDPDF
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.
Q2SL57
B8IYH2
RS10_DESDA
30S ribosomal protein S10
Desulfovibrio
MTTVSSDRIRIKLKAYDYRILDKAVAEIVDTARNTGAGVAGPIPLPTNIHKYTIQRSVHVDKKSREQFEMRIHKRLMDILEPTQQTVDALGKLSLPAGVDVEIKL
Involved in the binding of tRNA to the ribosomes.
B8IYH2
Q5R8M2
SUSD4_PONAB
Sushi domain-containing protein 4
Pongo
MYHGMNPSNGDGFLEQQQQQQPQSPQRLLAVILWFQLALCFGPAQLTGGFDDLQACADPGIPENGFRTPSGGVFFEGSVARFHCQDGFKLKGATKRLCLKHFNGTLGWIPSDSSICVQEDCRIPQIEDAEIHNKTYRHGEKLIITCHEGFKIRYPDLHNMVSLCRDDGTWNNLPICQGCLRPLASSNGYVNISEFQTSFPVGTVIYYRCFPGFKLDGSAYLECLHNLIWSSSPPRCLALEVCPLPPMVSHGDFVCHPRPCERYNHGTVVEFYCDPGYSLTSDYKYITCQYGEWFPSYQVYCIKSEQTWPSTHETLLTTWKIVAFTATSVLLVLLLVILARMFQTKFKAHFPPRGPPRSSSSDPDFVVVDGVPVMLPSYDEAVSGGLSALGPGYMASVGQGCPLPVDDQSPPAYPGSGDTDTGPGESETCDSVSGSPELLQSLYSPPRCQESTHPASDNPDTIASTAEEVASTSPGVDIADEIPLMEEDP
Acts as complement inhibitor by disrupting the formation of the classical C3 convertase. Isoform 3 inhibits the classical complement pathway, while membrane-bound isoform 1 inhibits deposition of C3b via both the classical and alternative complement pathways.
Q5R8M2
Q03D45
RS18_LACP3
30S ribosomal protein S18
Lacticaseibacillus
MAQQRRGGRRRRKVDFIAANHIEYIDYKDTNLLDRFISERGKILPRRVTGTSAKNQRKLTIAIKRARIMGLLPFVSED
Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit.
Q03D45
B2GHT4
PYRD_KOCRD
Dihydroorotate oxidase
Kocuria
MRLYPAFFKAAFSWMDPELAHTLGFAGIKLAHRTGLGRVLSRVTAPDEGAEVNVMGLTFPSPFGLAAGFDKGATGTHALTQLGFGHVEIGTVTGQAQPGNPRPRLFRLVRDRAVINRMGFNNDGAEAVAPRVAAALQTLAQESIRTGRRRPVVGVNIGKTKAVGLEDAAADYVRSTRVLAPYADYLVVNVSSPNTPGLRQLQELDALRPLLLAVRAEADRVTGRRVPLLVKIAPDLADEDVTAVADLALELGLDGIVATNTTIAREGLGLRTNHDDVAACGAGGLSGAPLRRRSLEVLRLLKEHAGEQLVLVSVGGVTTARDVMERLDAGASLVQGYTAFLYEGPFWAGRINRGLRRAAREGR
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
B2GHT4
Q2JM08
SSRP_SYNJB
Small protein B
unclassified Synechococcus
MAVDPNVKTLVDNRRARFEYDILETYEAGIQLTGTEVKSIRAGKANLQDAFALFRDGEAWLHNLHISPHDTASKVFNHDPTRRRKLLLHRREIDRLRGLVEQKGLTVVPLKLVLNRGWIKAHLGVARGKKLHDKRQAIKERQTQREIQRELKER
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.
Q2JM08
Q6MYT0
CHS7_ASPFU
Chitin synthase export chaperone
Aspergillus subgen. Fumigati
MGFGQFDSICQKAALPLCSLVGPSSPISGSTGIIPNCYARNIELANTIIFEGAASFVHIIALGMTVIMILHVRSKFTAVGRKEIITFFYIYMALTICSLVIDAGVVPPRSGPFPYFVAVQNGLSSALCTCLLINGFVGFQLYEDGTFLSVWLIRLTSAVMFVVSFLISLLTFKSWGGMSPTNTIALFVVLYILNAISIAIYLVMQLLLVMNTLEDRWPLGHIAFGVIVFICGQVLLYGFSDTICDNVQHYLDGLFFATFCNLLAVMMVYKFWDYITKEDLEFSVGIKPNTWEVKELLPEEDRRTTVYQDSHSEYAGSMYHHRASTYGGHNY
Chaperone required for the export of the chitin synthase chs3 from the endoplasmic reticulum.
Q6MYT0
E9Q9W7
PDZD7_MOUSE
PDZ domain-containing protein 7
Mus
MARGFTVGFDPLGLGELSSGSLSSVSSRGHLGSDSGSTATRYLLRKQQRLLNGPSRGIRASSPMGRVILINSPIEANSDESDIIHAVRVEKSPSGRLGFSVRGGSEHGLGIFVSKVEEGSSAERAGLCVGDKITEVNGLSLESTTMGSAVRLLTSSSCLHMMVRRMGRVPGIKFSKEKTTWVDVVNRRLVVEKCSSTPSDRSSEDGVRRIVHLYTTSDDFCLGFNIRGGKEFGLGIYVSKVDHGGLAEENGIKVGDQVLAANGVRFDDISHSQAVEVLKGQTHIMLTIKETGRYPAYKEMVSEYCWLDRLSNGVLQQLSPASESSSSVSSYASSAPCSSGSLPSDRMDVCLGPEEPTSHGPGWGRADTAMQTEPDLDSRVETWCSVRPTVILRDTAIRSDGPSSTRHLDSALSESPKTALLLALSRPRTPITRSQSHLTLWEEKKQRKKEKSGSSGEKGALQRSKTLMNLFFKGGRQGRPAGDGHREAWTLDSRSPTKVRPRLDLEKAGSVGPVQKFVTWRLRRDRERGRALLSARSGSPSGQAPTVNEQVQAWESRRPLIQDLARRLLTDDEVLAVTRHCSRYVHEGGVEDLVRPLLAILDRPTKLLLLRDIRSVVAPTDLGRFDSMVMPVELEAFEALKSRAVGPSALRPTRQDTPPKRHLITPVPDSRGGFYLLPVNSSEDEDGEIREKLGVLKVSLGASAPHHKGIPPLQDVPVDAFSLRRGACAPPPQPPPVAPRPPRPNWLLTEPLSREDTQQNQSQTPAQSCSRSRSRSRSRSHSRGQGKSPGRRRSPSPAPIATAATANGRYHRPRKARPLLPRLLDGQVAKVGARQGPLENGRIAEEAVGNVSTGALRTITLSKMKQSLGISISGGIESKVQPMVKIEKIFPGGAAFLCGDLQAGFELVAVDGESLEQVTHQRAVDTIRRAYRNKAREPMELVVRVPGPGLLPLASDLRVVKDQSLAPDCPSALGPVDDARILTQLPPPEARQLQQSLSSALKVPQSIPKLSPILKDPHDPS
In cochlear developing hair cells, essential in organizing the USH2 complex at stereocilia ankle links . Blocks inhibition of adenylate cyclase activity mediated by ADGRV1 .
E9Q9W7
B0BRX8
ATP6_ACTPJ
F-ATPase subunit 6
Actinobacillus
MAGTTAEYISHHLSFLASGDGFWAVHLDTLFFSLLAGVIFLFVFSRVAKNATSGVPGKLQCFVEIVIGWVDGLVKDNFHGPRNVIAPLALTIFCWVFIMNAIDLVPVDFLPQLANMFGIHYLRAVPTADISATLGMSICVFFLILFYTVKSKGFGGLVKEYTLHPFNHWAFIPVNFILETVTLLAKPISLAFRLFGNMYAGELIFILIAVMYMADNFALQALGIPLHLVWAIFHILVITLQAFIFMMLTIVYLSIAYNKADH
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
B0BRX8
Q1DKL9
CLP1_COCIM
mRNA cleavage and polyadenylation factor CLP1
Coccidioides
MSLPGLELSQQPIEARRAPPQPTQISLPKGSEWRFEVAFGNTTRVKLLAGTAELFGTELATSQTYTFSGTKAAIYTWHGCTLEVGAGDPVPIGPVGSAPVPPGPGNGGCQVEYIAEETPMAEYANVHFALETMRHDAKAAGRDGPRVLILGPEDAGKTSLAKILTGYATKMGRQPLVVNLDPSEGMLSVPGALTATAFRSMIDVEEGWGSSPMSGPSPIPVKLPLVYFYGLPACLDGDGSYYKAIVSRLALAVTGRMAEDSDAREAGVIIDTPGIIGQGKGASEDVIHHIVTEFSISTILVIGSERLYSTMVKNYDNKPIATSATAAASDERISVVKLTKSGGCVDRDATFMKYVRESQIRSYFFGSPVPSTASSALSLSSTTTGTTMTLSPHTSQVDFNSLSIYSITIATEGEEDEYDPSKFDSFLPGGHEENDHNTSLTGTTSLQPPSGLLPGLRSELPSATTGFPSASTSSTTPFTNLPSPAPMSLANTLLAITNAAPNASLDEVRDASIMGFIYIADVDEKKGQGGKLRLLAPVGGRVPNRAMIWGRKWPGEVVGLIG
Required for endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation.
Q1DKL9
P26273
LHA_ROSDO
Antenna pigment protein alpha chain
Roseobacter
MAKFYKIWLIFDPRRVFVAQGVFLFLLAAMIHLVVLSSGLNWFEAAAAVGGQ
Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
P26273
O66728
AATNT_AQUAE
A-adding enzyme
Aquifex
MVCPKVVILSEGADLDSLSAAYGVLKLYPDAYLLKPKHLSKKAGEVFKKYRDKFRVIEDLPDCFELVLVDTHFLPEGLPRERIKRIIVYDHHPIGDVKEFEGKIEKVGAATTLVVEEIKEKGIDINPRDATLLAFGIYEDTGNFTYEGTTPRDALALAFLLEKGANLREIREVVMETYTPEQIEAVGKIVQSIEKVFINGRQISFATAVLERYQPDINTLLYEIKDLKESDAFFVIIEAEGKTYVFGRSQSEDVDVGEILSHFGGGGHREAGAVKLENVSAERIKELIKAFLKRKYVKLKVRDIMNTPPFVLEEHVSVKDALTELSERGIANAPVINREGKLVGIISKKALLKLVKLYPDEPIELFVNRDFYTLSPDAPVWEAEEILTKFGQKLIPVVEDGTVVGVVTRLDILQAVKEDLEKLKEKRRKIKVPENIEEIAREVGQIAKEMGLRAYIVGGVVRDILLGKEVWDVDFVVEGNAIELAKELARRHGVNVHPFPEFGTAHLKIGKLKLEFATARRETYPRPGAYPKVEPASLKEDLIRRDFTINAMAISVNLEDYGTLIDYFGGLRDLKDKVIRVLHPVSFIEDPVRILRALRFAGRLNFKLSRSTEKLLKQAVNLGLLKEAPRGRLINEIKLALREDRFLEILELYRKYRVLEEIIEGFQWNEKVLQKLYALRKVVDWHALEFSEERIDYGWLYLLILISNLDYERGKHFLEEMSAPSWVRETYKFMKFKLGSLKEELKKAKENYEVYRLLKPLHTSVLLLLMLEEELKEKIKLYLEKLRKVKLPKEKIEELKKQGLKGKELGERIEELKREIMNKI
tRNA nucleotidyltransferase involved in the synthesis of the tRNA CCA terminus. Adds the terminal adenosine residue to tRNA . Can incorporate CMP into tRNA ending with C74C75 (tRNACC), with very weak efficiency .
O66728
B5QZS9
GATZ_SALEP
D-tagatose-1,6-bisphosphate aldolase subunit GatZ
Salmonella
MKEIISRHKAGEQIGICSVCSAHPLVIESALRFDLNSGNKVLIEATSNQVNQFGGYTGMKPADFRDFVYGIAQEVGFPRERLILGGDHLGPNCWQNEPADTAMEKSVELIKAYVAAGFSKIHLDASMSCADDPTPLDPMVVAKRAALLCQAAETTATDEQKRHLTYVIGTEVPVPGGEASAINAVHVTREQDAARTLQTHQAAFRALGLDEALNRVIAIVVQPGVEFDHTQIIHYQPQAAQALSAWIKETPMVYEAHSTDYQTRQAYRALVRDHYAILKVGPALTFALREAIFALAQMENELISPEQRSRVLEVIDEVMLNEPGYWKKYYRPTWSQAMVDIHFSLSDRIRYYWPHPRIRQSVEKLIANLNNVTLPLGLISQFMPVQFERLSEGVLTPTPHNLIIDKIQDVLRAYRFGCTPDVA
Component of the tagatose-1,6-bisphosphate aldolase GatYZ that is required for full activity and stability of the Y subunit. Could have a chaperone-like function for the proper and stable folding of GatY. When expressed alone, GatZ does not show any aldolase activity. Is involved in the catabolism of galactitol.
B5QZS9
P06574
RPSB_BACSU
null
Bacillus
MTQPSKTTKLTKDEVDRLISDYQTKQDEQAQETLVRVYTNLVDMLAKKYSKGKSFHEDLRQVGMIGLLGAIKRYDPVVGKSFEAFAIPTIIGEIKRFLRDKTWSVHVPRRIKELGPRIKMAVDQLTTETQRSPKVEEIAEFLDVSEEEVLETMEMGKSYQALSVDHSIEADSDGSTVTILDIVGSQEDGYERVNQQLMLQSVLHVLSDREKQIIDLTYIQNKSQKETGDILGISQMHVSRLQRKAVKKLREALIEDPSMELM
Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. Sigma B is not essential for sporulation; rather it is required for maximal expression of ctc and csbA which are transcribed in the early stationary phase under conditions inimical to sporulation. May play a role in the ability of the bacterium to adapt to various stresses but is not essential for its survival under these conditions. Positively regulates expression of its own operon. The second most abundant sigma factor, it associates with RNAP core under all growth phases .
P06574
P01474
3SOF2_NAJME
Cytotoxin homolog V-II-2/V-II-3
Naja
IKCHNTLLPFIYKTCPEGQNLCFKGTLKFPKKTTYNRGCAATCPKSSLLVKYVCCNTNKCN
Has low cytotoxic activity.
P01474
Q2JMJ0
PSTB1_SYNJB
Phosphate-transporting ATPase 1
unclassified Synechococcus
MRPPFPGTPDSSKKSANLTVKLETQAVSVYYGSHLAVKQVSLKIPKNHITAFIGPSGCGKSTLLRCFNRMNDLIPGARVEGSVIFHGKNIYDPDVDPAEVRRRVGLVFQKPNPFPKSIYDNIAFGPRVNGYQGDLDELVERALRQAVLWDEVKDKLKTSGLSLSGGQQQRLCIARTLAIQPEVILMDEPCASLDPISTLRIEELLKELGRRYTIIIVTHNMQQAARVSDFTAFFNTEVDEEGFRYGRLVEFNRTEKIFNSPAHRETEEYVSGRFG
Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Q2JMJ0
A9AAX4
DNLI_METM6
Polydeoxyribonucleotide synthase [ATP]
Methanococcus
MLFIDFCKILDKIEKTTKRLEKTDYFVELIDFIKNNGKAENLKQVSQITIGRVFAEFENKEIGIGPNLLIEAVKTTGISEKDLKAEIKKTGDIGIAVENLSSNIKQVSLFSQPLTLEEIYSTLKKLSEIEGNSSQKKKTRIISNLLILSNPVESRYISRLILEDMRIGMNIPTILASFSNYFNVNKEAVEKIYAVTNDIGLIGKKLISGSDIENDSELKLKVFRPIKPMLAQLTPSIEDAIIETKMPQFETKYDGARVQVHKSNGKVNIYSRRLENITNSVPELVEEINKIDIDNIILEGECVAMDLSSGKPRPFQDILRRFRRKYDIDKVAEKIALRIYFFDVLYYEKGLIDTPLKNRREILEKLFGTNNWDSELEKIQKEIFSNKMLFSSFKLNSDDPDLAKEFFNWSLSIGHEGIMIKNPDAPYTPGSRVKTMYKVKPTLENLDVVVTRAKIGMGKRKDWYGSYEISVKDDEDNLHVIGNVGSGLTEDDLERLTTIVNEIKIEDLGEEVILEPKIVLEVTYEEIQTSEKYEMGYALRFPRVVQIREDKSINDINTLDDVKKIYEIERNRK
DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.
A9AAX4
Q8Q0B5
THI4_METMA
Thiamine thiazole synthase
Methanosarcina
MELDEVIITRAIFEEYSKTFLEYTDIDVALVGGGPANLVAAKYLAEAGAKVAIYEQKLSLGGGMWAGGMMFPRIVVQEEACRVLDDFGIRYKEYEPGYFVANSVESVGKLIAGATSAGAEVFNLVSFEDIMIRENDRVTGIVINWGPVTTQRLHVDPLMIRTKLVIDGTGHDAVVCNTILRKIPNAKIGEFGILGEKPMWSEVGERLAVDATQEIYPGLIVAGMAANAATRAPRMGPVFGGMLLSGEKAAKLALDRLKKI
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.
Q8Q0B5
A8NF99
CPF2_COPC7
Siderophore biosynthesis protein cpf2
Coprinopsis
MSADDVVYDLVGLGFGPANIAIGAALTEKWQQDPTFSIKNTLFIEKHEVFRWHPGMLLPDAKMQISFLKDLATLRTPNSPYTFLSYLHSEDRLLSFINRGSTVPSRKEYSDYLAWAAQKVQDNGVKVKFGHEIIALDDGPDGTIEVRYRNVRTQEETLIRARDLIIAPGGTPCIPDFLQPFVNHPRVSHSSSYALKIGDMFDSLNHLSRPLRVAIIGSGQSAAEVTIDVRNRLASIPSTGRHEVDMLIRKGSLKPSDDSPFANEIFDPASTDAWFSTGSKHLRDAILAEYKQTNYSVVNPRTLEALYEIIYGQRLNAAVSRRTNVEEPSDPVINIKPYTSVLSIQTVGSQGERVRGELLLSPEGASASKDEGFVMVTKHMMTGAESQTNYDVILYATGYQRTAWVELFKNTGIAKHFGITPSTSKVVLRPSADLVGGRQHQEFFHDSSPSTASSSTVSTPPTSPETSRFSSPISSRIVSQDLYLSRSYQLLPKDGENTLRPRVYLQGVEEATHGLSDTLLSVLGVRAGEVVADLASRYHSSA
L-ornithine N(5)-monooxygenase; part of the gene cluster that mediates the biosynthesis of coprinoferrin, an acylated tripeptide hydroxamate siderophore . The biosynthesis of coprinoferrin depends on the hydroxylation of ornithine to N(5)-hydroxyornithine, catalyzed by the monooxygenase cpf2 . The second step, the acylation of N(5)-hydroxy-L-ornithine to yield N(5)-hexanoyl-N(5)-hydroxyl-L-ornithine is catalyzed by a not yet identified acyltransferase (Probable). Finally, assembly of coprinoferrin is catalyzed by the nonribosomal peptide synthase (NRPS) cpf1 via amide bond formation between three N(5)-hexanoyl-N(5)-hydroxyl-L-ornithine molecules to release the linear trimer . Interestingly, proteins seemingly not directly related to biosynthesis, such as transcription factors, replication factors, and autophagy-related proteins, are conserved among the clusters homologous to the coprinoferrin cluster, suggesting that the cluster may also play developmental and cell biological functions (Probable).
A8NF99
B3E610
PROB_TRIL1
Gamma-glutamyl kinase
Trichlorobacter
MRRGLLQQVRRVVIKVGSRVLTVEGGGLDYDAISRLCDEMAGLRQQGIEVILVSSGAVAAGRDALRSADTTLTIPQKQAAAAVGQPLLMQAYQQACTRHGLVTAQILLTAEDLANRNRFLNARTTLEALLTAGALPVINENDSVAVAEIKFGDNDNLSALVTSLAEADLLLILTDIEGLYSANPASDPDAELIPLVRSITREIERMAGGSGSNVGTGGMATKVTAAKKAARFGVPTILAPGKQPGVITAAVSGQEIGTLFLPATDGLNRRKHWIAYTLRPAGKVLVDAGAQKALVEKGTSLLPSGITGVEGRFERGRCVRICGPDGTEIARGLADYSSSEIQLIAGHKSAEIEQLLGYRYGDDVVHRDNLVLMTHS
Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
B3E610
A1VQF4
SURE_POLNA
Nucleoside 5'-monophosphate phosphohydrolase
Polaromonas
MKILICNDDGYQASGIVALYEALKTIADVEVVAPEQNNSAKSNALTLHSPMYVQTAANGFRYINGTPADCVHIALTGLLGYRPDLVVSGINNGANMGDDTIYSGTVGAAMEGYLFGIPAIAFSQTEKGWTHIDVAAQQARNLIKQLIPSLEAVAEGAQPSVPPWLLNVNIPNLPAGQVEGFKVCRLGRRHAAERVIVQTSPRGESMYWIGGAGPAKEAGEGTDFHATTQGYVSITPLHVDLTDHERLPYWAQTAARLTHKH
Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
A1VQF4
Q0AFX7
EX7L_NITEC
Exodeoxyribonuclease VII large subunit
Nitrosomonas
MTDNNLFPEPKKIVWRVSELNRHVRVILEQTFPLLWVSGEISNLKRYPSGHWYFSLKDDNAQVRCVMFRHKNMYLDWMPQDGAQVEAQALITLYEARGEFQLTIERLRRAGLGVLFETFERLKTRLQQEGLFNPEYKQLIPPYPQQIGIITSTNTAALRDVLTTLQRRLPSLPVVIYPAPVQGKEAASAIVTALQIATQRSECDVLILCRGGGSIEDLWAFNEEIVARAIAACPIPIVTGIGHETDFTIADFVADMRAPTPTGAAQLAAPDRQDILHRLQYWQHRLQQAIERNIERRMQTTDLLAHRLVHPGERIRYQLIHLSQLHNRLLHAWSRQLEVCKWRIEAFRRRIQFTKPDINTGKRYQQELAARLQRAMVYRLESLQVQLIRQQQHLAHLDPKAVLERGYSITYTAGGEILQDSQQIHTGDNVQIVFAKGSAKANITETNK
Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Q0AFX7
Q8FL93
RLUA_ECOL6
tRNA pseudouridine(32) synthase
Escherichia
MGMENYNPPQEPWLVVLYQDDHIMVVNKPSGLLSVPGRLEEHKDSVMTRIQRDYPQAESVHRLDMATSGVIVVALTKAAERELKRQFREREPKKQYVARVWGHPSPAEGLVDLPLICDWPNRPKQKVCYETGKPAQTEYEVVEYAADNTARVVLKPITGRSHQLRVHMLALGHPILGDRFYASPEARAMAPRLLLHAEMLTITHPAYGNSMTFKAPADF
Dual specificity enzyme that catalyzes the synthesis of pseudouridine from uracil-746 in 23S ribosomal RNA and from uracil-32 in the anticodon stem and loop of transfer RNAs.
Q8FL93
Q9UT91
RMP1_SCHPO
RNA-processing protein rmp1
Schizosaccharomyces
MQELQYDVVLLQKIVYRNRNQHRLSVWWRHVRMLLRRLKQSLDGNEKAKIAILEQLPKSYFYFTNLIAHGQYPALGLVLLGILARVWFVMGGIEYEAKIQSEIVFSQKEQKKLELQSQDDIDTGTVVARDELLATEPISLSINPASTSYEKLTVSSPNSFLKNQDESLFLSSSPITVSQGTKRKSKNSNSTVKKKKKRARKGRDEIDDIFG
Functions as part of ribonuclease MRP (RNase MRP), which is involved in rRNA processing in mitochondria.
Q9UT91
G8BAW7
FAS2_CANPC
Beta-ketoacyl synthase
Candida
MKPEIEQELSHTLLTELLAYQFASPVRWIETQDVFLKQHNTERVIEIGPSPTLAGMASRTIKAKYQSYDAALSLQRQVLCYSKDAKEIYYTPDPAEPPAAEEPKAETGKESAPAASAAAAAATQPAAAVAPPPQSAGPVESIPDEPVKASLLIHVLVAQKLKKPLDAVPMSKAIKDLVNGKSTVQNEILGDLGKEFGSTPEKPEETPLEELAEQFQDTFSGSLGKTSTSLIGRLMSSKMPGGFSITNARKYLESRFGLGPGRQDSVLLTALCNEPASRLGSEGDAKSFLDTMAQKYASHAGISLSSPSAGGASSGAGAAVVDSAALDALIAENKKLARQQLETLARYLQVDLTKGEKAFIKEKEATTVLQQELDLWEAEHGEFYAKGIKPVFSPLKSRTYDSYWNWARQDLLSMWFDILFGKLTSVDRETINQCIQIMNRANPTLIKFMQYHVELCPTYRGETYKLGKRLGEQLIENCKQILGQSPVYKDVSRITGPKTTVSAKGDIVYEEANKESVRKFEQYVFEMAQGGSMTKMKQSSIQEDLARVYKAISKQASRDSKLELQKVYDQLLKVVEGSTEIETEQTTQDALAIPTGSNTPTEEDELSTASDDDEIASLPDKTSIAQPVSSTIPNKTIPFLHIQSKSESGNWEYDRKLSSIYLDGLESAAINGLTFKDKYVLVTGAGAGSIGAEILQGLISGGAKVIVTTSRYSKKVTEYYQNMYARYGAAGSTLIVVPFNQGSKQDVDALVEYIYNDQKKGGLGWDLDVIIPFAAIPENGNGIDNIDSKSEFAHRIMLTNLLRLLGAVKARKTTDTRPAQCILPLSPNHGTFGFDGLYSESKISLETLFNRWYSEDWGTKLTICGAIIGWTRGTGLMSANNIIAEGIEKLGVRTFSQKEMAFNILGLLTPEIVNLCQEEPVMADLNGGLQFIDNLKEFTSKLRNDLTETADIRRAVSIESAIEQKVVNGDNVDSNYNKVTVRPRANMKFDFPTLKSYDEIKQIAPDLEGMLDLENVVVVTGFAEVGPWGNARTRWEMESKGEFSLEGAIEMAWIMGMIKYHNGNLKGKPYSGWIDAKTQTPVDDKDIKAKYEEEILEHSGIRLIEPELFNGYDPKKKQMIQEVVIQHDLEPFECSKETAEQYKHEHGDKCEISEIEESGEYSVRILKGATLFIPKALRFDRLVAGQIPTGWDARTYGIPEDTINQVDPITLYVLVATVEALLSAGITDPYEFYKYVHVSEVGNCSGSGMGGVSALRGMFKDRYADKPVQNDILQESFINTMSAWVNMLLLSASGPIKTPVGACATAVESVDIGIETILSGKAKVVMVGGYDDFQEEGSYEFANMNATSSAIDEFKHGRTPKEMSRPTTTTRNGFMEAQGSGIQVIMSADLALKMGVPIHAVLAMSATATDKIGRSVPAPGKGILTTAREHHGNLKYPSPLLNVKYRKRQLSKRLDQIKSWESSELNYLQEEAHLAKEEFGEEFSEAEFLRERTEEIYRESKRQVADAKKQWGNAFYKSDPRIAPLRGALATFNLTIDDIGVASFHGTSTVANDKNESATIDSMMKHLGRSEGNPVFGVFQKYLTGHPKGAAGAWMLNGAIQILESGIVPGNRNADNVDKVLEQYEYVLYPSRSIQTDGIKAVSVTSFGFGQKGAQAVVVHPDYLYAVLDRSTYEDYAKRVTARNKKTYRYMHNAITRNTMFVAKDKAPYSDELTMDVYLDPLARVSKTKNEFVFTKKSVQSDKSYVSNIANSTAKALSSLNKSSKGVGVDVELLSELNIDNETFLERNFTPEEIKYCQNSANPQASFTGTWSAKEATFKALGVSSQGGGASLKEIEIVRDGNGAPQVVLNDNAKAAAKAAGVKNVNVSISHDDFQATAVALSEF
Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase.
G8BAW7
Q8KTA9
SECE_RICBE
Protein translocase subunit SecE
belli group
MFKEYKIYKFFEQVKQEAYKVVWPTKKELTASTLVVIVAVFVFSLICLVLDYGIHNIIQILLNIGK
Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Q8KTA9
Q73SS0
HEM3_MYCPA
Pre-uroporphyrinogen synthase
Mycobacterium avium complex (MAC)
MIRIGTRGSLLATTQAGGVRDALIARGHPAELVTITTAGDRSSGPIESLGVGVFTTALREAIEEGRVDAAVHSHKDLPTADDPRFAVAAIPARNDPRDAVVARDGLVLAELPPGSLVGTSSPRRAAQLRALGLGLEIRPLRGNLDTRLNRVSSGDLDAIVVARAGLARLGRLGDVTETLEPVQMLPAPAQGALAVECRAGDSRLAAVLAELDDADTRASVTAERALLAELEAGCSAPVGAIAEVVESIDEDGRIFEELSLRGCVAALDGSDVIRASGIGTPGRARELGLSVAAELFELGARELMSGARHDPARGN
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Q73SS0
Q9CPX6
ATG3_MOUSE
Autophagy-related protein 3
Mus
MQNVINTVKGKALEVAEYLTPVLKESKFKETGVITPEEFVAAGDHLVHHCPTWQWATGEELKVKAYLPTDKQFLVTKNVPCYKRCKQMEYSDELEAIIEEDDGDGGWVDTYHNTGITGITEAVKEITLESKDSIKLQDCSALCDEEDEEDEGEAADMEEYEESGLLETDEATLDTRKIVEACKAKADAGGEDAILQTRTYDLYITYDKYYQTPRLWLFGYDEQRQPLTVEHMYEDISQDHVKKTVTIENHPHLPPPPMCSVHPCRHAEVMKKIIETVAEGGGELGVHMYLLIFLKFVQAVIPTIEYDYTRHFTM
E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt), autophagy, and mitochondrial homeostasis. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A). The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8-like proteins from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8-like proteins. The formation of the ATG8-phosphatidylethanolamine conjugates is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). Preferred substrate is MAP1LC3A. Also acts as an autocatalytic E2-like enzyme, catalyzing the conjugation of ATG12 to itself, ATG12 conjugation to ATG3 playing a role in mitochondrial homeostasis but not in autophagy. ATG7 (E1-like enzyme) facilitates this reaction by forming an E1-E2 complex with ATG3. ATG12-ATG3 conjugate is also formed upon viccina virus infection, leading to the disruption the cellular autophagy which is not necessary for vaccinia survival and proliferation. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway.
Q9CPX6
B3PPK3
CHED_RHIE6
Probable chemoreceptor glutamine deamidase CheD
Rhizobium
MITEGAARRVHIIQGEYKVLSDPNAVLSTILGSCVAACLRDPVAGIGGMNHFLLPGSATSPTSGGDATRYGVHLMELLINGLLKQGARRDRLEAKIFGGAKTISTFSNVGEQNAAFAMQFLRDEGIPVVGSSTGGEHGRKLEYWPVSGRARQYPLTGAETQRTVALEQRPAAPQKPVETSIEFF
Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
B3PPK3
Q8E281
RBSA_STRA5
Ribose import ATP-binding protein RbsA
Streptococcus
MKIDMRNISKSFGTNKVLEKIDLELQSGQIHALMGENGAGKSTLMNILTGLFPASTGTIYIDGEERTFSNPQEAEEFGISFIHQEMNTWPEMTVLENLFLGREIKTTFGLLNQKLMRQKALETFKRLGVTIPLDIPIGNLSVGQQQMIEIAKSLLNQLSILVMDEPTAALTDRETENLFRVIRGLKQEGVGVVYISHRMEEIFKITDFVTVMRDGVIVDTKETSLTNSDELVKKMVGRKLEDYYPEKHSEIGPVAFEVSNLCGDNFEDVSFYVRKGEILGFSGLMGAGRTEVMRTIFGIDKKKSGKVKIDDQEITITTPSQAIKQGIGFLTENRKDEGLILDFNIKDNMTLPSTKDFSKHGFFDEKTSTTFVQQLINRLYIKSGRPDLEVGNLSGGNQQKVVLAKWIGIAPKVLILDEPTRGVDVGAKREIYQLMNELADRGVPIVMVSSDLPEILGVSDRIMVMHEGRISGELSRKEADQEKVMQLATGGK
Part of the ABC transporter complex RbsABC involved in ribose import. Responsible for energy coupling to the transport system.
Q8E281
A4VNY2
ISCS_PSEU5
Cysteine desulfurase IscS
Pseudomonas
MKLPIYLDYSATTPVDPRVAEKMIECLTNEGNFGNPASRSHAFGWKAEEAVENARRQVAELVNADPREIVWTSGATESDNLAIKGVAHFYASKGKHIVTTKIEHKAVLDTTRQLEREGFEVTYIEPGDDGIVTPAMVEAALREDTILVSVMHVNNEIGTINDITAIGELTRARGILFHVDAAQSTGKVEIDLEKIKVDLMSFSAHKTYGPKGVGALYVRRKPRVRLEAQMHGGGHERGMRSGTLATHQLVGMGEAFRIAKQEMAQENERIRALRDRFYKQVEHLEELYVNGSMTARVPHNLNLSFNYVEGESLIMALKDLAVSSGSACTSASLEPSYVLRALGRNDELAHSSIRFTFGRFTTEEEIDYAAQKVCEAVTKLRELSPLWDMFKDGVDISKVEWQAH
Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins.
A4VNY2
Q1HUV6
CYB_STUER
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
Sturnira
MTNIRKTHPLLKIINNSLVDLPAPSSLSSWWNFGSLLGVCLGVQILTGLFLAMHYTSDTATAFNSVTHICRDVNYGWLLRYLHANGASMFFICLYLHVGRGLYYGSYTYSETWNIGILLLFAVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTELVQWIWGGFSVDKATLTRFFAFHFLLPFIVAALVMVHLLFLHETGSNNPTGIPSDPDMIPFHPYYTIKDILGFLVMLTALSALVLFSPDLLGDPDNYIPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSILILTIVPILHMSKQRSMMFRPLSQCLFWLLVAVLFTLTWIGGQPVEHPYIIIGQTASVLYFLILLVLMPLTSITENHLLKW
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.
Q1HUV6
Q46899
CASC_ECOLI
CRISPR system Cascade subunit CasC
Escherichia
MSNFINIHVLISHSPSCLNRDDMNMQKDAIFGGKRRVRISSQSLKRAMRKSGYYAQNIGESSLRTIHLAQLRDVLRQKLGERFDQKIIDKTLALLSGKSVDEAEKISADAVTPWVVGEIAWFCEQVAKAEADNLDDKKLLKVLKEDIAAIRVNLQQGVDIALSGRMATSGMMTELGKVDGAMSIAHAITTHQVDSDIDWFTAVDDLQEQGSAHLGTQEFSSGVFYRYANINLAQLQENLGGASREQALEIATHVVHMLATEVPGAKQRTYAAFNPADMVMVNFSDMPLSMANAFEKAVKAKDGFLQPSIQAFNQYWDRVANGYGLNGAAAQFSLSDVDPITAQVKQMPTLEQLKSWVRNNGEA
A component of Cascade, which participates in CRISPR interference, the third stage of CRISPR immunity. Cascade binds both crRNA and in a sequence-specific manner negatively supercoiled dsDNA target. This leads to the formation of an R-loop in which the crRNA binds the target DNA, displacing the noncomplementary strand. Cas3 is recruited to Cascade, nicks target DNA and then unwinds and cleaves the target, leading to DNA degradation and invader neutralization. CasCDE alone is also able to form R-loops.
Q46899
Q9X0M7
MCP2_THEMA
Methyl-accepting chemotaxis protein 2
Thermotoga
MSLKGKTLLVSTITLAAVVLVALLGGSVFLKAGQNVRKAFEEYELAVEALDKLGELETKVALFVNNAAKIEEVSSLFNELKKVADKIPSLKEHMDALERNISEIISGKTEVVSRIQSSVDQVKEDIMANLDRTRENLDKEISYSSELIRNVLFIVLPIVAVASGVFLFVMISRSLRLLKPVMEASRSLRNNDLTINIQEAKGKDEISTLLNEFKASIEYLRNNLKDVQTETFSVAESIEEISKANEEITNQLLGISKEMDNISTRIESISASVQETTAGSEEISSATKNIADSAQQAASFADQSTQLAKEAGDALKKVIEVTRMISNSAKDVERVVESFQKGAEEITSFVETINAIAEQTNLLALNAAIEAARAGEAGRGFAVVADEIRKLAEESQQASENVRRVVNEIRSIAEDAGKVSSEITARVEEGTKLADEADEKLNSIVGAVERINEMLQNIAAAIEEQTAAVDEITTAMTENAKNAEEITNSVKEVNARLQEISASTEEVTSRVQTIRENVQMLKEIVARYKI
Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation.
Q9X0M7
Q9BVM4
GGACT_HUMAN
Gamma-glutamylamine cyclotransferase
Homo
MALVFVYGTLKRGQPNHRVLRDGAHGSAAFRARGRTLEPYPLVIAGEHNIPWLLHLPGSGRLVEGEVYAVDERMLRFLDDFESCPALYQRTVLRVQLLEDRAPGAEEPPAPTAVQCFVYSRATFPPEWAQLPHHDSYDSEGPHGLRYNPRENR
Contributes to degradation of proteins cross-linked by transglutaminases by degrading the cross-link between a lysine and a glutamic acid residue. Catalyzes the formation of 5-oxo-L-proline from L-gamma-glutamyl-L-epsilon-lysine. Inactive with L-gamma-glutamyl-alpha-amino acid substrates such as L-gamma-glutamyl-L-alpha-cysteine and L-gamma-glutamyl-L-alpha-alanine.
Q9BVM4
P24129
FUSD_BURCE
Fusaric acid resistance protein FusD
Burkholderia cepacia complex
MNDALALLLSMLVSAIAFAVLFPPTAPWLKKRLFADLRHQAVAACHARLAGLRTRFESGARDLMYQAHTLSADHPTCSATPCWMFAVLETGNAAIDLRHELATLPSDPRYAPTTPWRRAIETMRAALSSLFARPDAERFDATLAAVNDAIDATRQTLDAFTPTREERHRLQRILSHLHFVRTALLDPESPLAALNRNRPVRPQPGASS
Involved in the resistance (detoxification) of the fungal toxin fusaric acid.
P24129
Q9ZEY9
REPA2_BUCAI
Probable replication-associated protein repA2
Buchnera
MPRKNYIYNLKPFFNPSKNERKKSTFICYAMKKVSEIDVARSHLNRALLPIDPKTGNVLPRFRRLNKHRACAMRAIVPAMLYYFNINSKLVEASIEKLADECGLSTLSDSGNKSITRASRLISEFLEPMGFVKCKKINSKSMSNYIPKKIFLTPMFFMLCGISPSEINHFLSKKIKPLKKLKKQEKSAFISFTDMKIISQLDERSARTKILNALINYYTASELTKIGPKGLKKKIDIEYSNLCNLYKKKS
This protein is essential for plasmid replication; it is involved in copy control functions.
Q9ZEY9
A8G6B7
DDL_PROM2
D-alanylalanine synthetase
Prochlorococcus
MIGEKKKRIGLIFGGYSNEHEVSISSAKTVFQAFNSEINKKRFKVKSFYIDKYGDWLDNDLSEKILNDEIKSNNIKKQEIVNQQKINFLDGIEFQNIDVWFPLLHGLNGEDGSIHGLLQYTRKPIVGCGILGSAIGMDKIMMKTIFSNLKIPQVNYLAFQNEDLDDREVKKKVINEILKKLNFPFFVKPSNSGSSLGISKVINESEILQSLEKAQKIDSRILVEEGLEVREIECGIIGNSELLTSEIGEIKYESDWYDYDSKYYSNNKIIIPAEIDSKITKEIKKIAIQSCRALNIFGFARVDFFLEKSSNKILLNEINTIPGFTTNSMFPMLWKASGLNIEQLVAKLVDISLDL
Cell wall formation.
A8G6B7
P22564
RIHC_ECOLI
Purine/pyrimidine ribonucleoside hydrolase
Escherichia
MRLPIFLDTDPGIDDAVAIAAAIFAPELDLQLMTTVAGNVSVEKTTRNALQLLHFWNAEIPLAQGAAVPLVRAPRDAASVHGESGMAGYDFVEHNRKPLGIPAFLAIRDALMRAPEPVTLVAIGPLTNIALLLSQCPECKPYIRRLVIMGGSAGRGNCTPNAEFNIAADPEAAACVFRSGIEIVMCGLDVTNQAILTPDYLSTLPQLNRTGKMLHALFSHYRSGSMQSGLRMHDLCAIAWLVRPDLFTLKPCFVAVETQGEFTSGTTVVDIDGCLGKPANVQVALDLDVKGFQQWVAEVLALAS
Hydrolyzes both purine and pyrimidine ribonucleosides with a broad-substrate specificity with decreasing activity in the order uridine, xanthosine, inosine, adenosine, cytidine, guanosine.
P22564
Q3ACY1
UPPP_CARHZ
Undecaprenyl pyrophosphate phosphatase
Carboxydothermus
MNSFQALILGLVQGLTEYLPVSSSGHLVLLQKIFGLKENVLLFDILVHLGTLVPLLIIFRDEILAIIKKPWGRLPLLIIAGTVPTALIGLGFKDFFERLFVSGSTLGIEFIITGLILWLAERQKSGRKNLEKTTFLDAIFVGVAQGLAILPAISRSGLTISGALIRGLNREWAAKFSFLLSIPAILGAAVLDLKSFVEQNANLAGIDLMPFIVGFFAAMLSGYFAVKFMLEILRKGKLTWFSYYVWILGVTILVLQAAGKF
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Q3ACY1
Q51ZN8
ATG2_MAGO7
Autophagy-related protein 2
Pyricularia
MATLFQSFRGSAMPKRLLRYALARLDLLDSDALDLDNLDLAIGRNTVLEFRDVGIKLPKLAKLLGLPPTFTLLKAKVILLRVTIPMDIYSSSLKIEVDRVDVQLKVDSKDDIDGRSRTTIRGPTDVVPNTVDLAQSFLEQQSPKEKEELEAALSAETQDVGGSLVLGEDEDEQDEGSYGTGQALSLPAFLANFLQGIVDRTQIQIRGVTFQLDVSVPLEPNLNAPDVVTVKLALGQIDVEGVTTSLGSDEQDRPKFVHKEGKRLVSLQDITAFLISEANVFSTFERTTSVPPSLSPQSSAASALRSPVSRESTSMPFQEQEVEGRSTQLPSFEDNLGDSEAALNIPYDLSDEDDQEPGNKTAASSMSTPRASILHDHLAHQDESSSFLQGFTPYTAATPGIHLDADQMDEMSPQPAHDLSTHNQISLSNSVLSNSSSGSSGQEPTEDLTESHLYTHEDAESMYMSAFSQHEPTPQSVVPNELYIDPSESSVGVSSPQGTRDEPSSSLGATYGLEDSQASSTIGFQGLKTSPGLDASTISEQSDSSPAPIIPPSSDGNTEAGPESSIQGERHDRKSQSPNECLTPREPTRLAKKVLALDTLSLYLPSSQKSVHVVPLDGQSSPGEPQPLSPSLASSVFPHVPGAFGASTSLPPSPPPISPTSIELDNQEPNDGILEAILSPISIQFDASIGFILAMVVSRLLGAISPSKEEPAQQTAKDNPSATNQATDHQAVKVTLQAVSILFLERLGGVSEAPDSIFGVRTSKFDEDILLQAQLRNVQCLLSSDETVIDAEGFTFGYAGDDNHIISFDRSKEMMASVKDAVPSPGSEVSIKLKKGGPSSKIDIATLPLQICLDLRRLDETFSWFGGLSSFLNMGSSIASINGIGNSQPAKPPARPASRGVKFDTPINPDDRSATSDNKINMRINTVRLDLIGKDCNVILETSAFKLVSRDEGIGIALRKIQVHGPYSNESGPHPPISVTITGSRIEYSMTPKEADLERLLELISPSKLRDTPDDDEIMVDTLLRQRRKGSVLRLKFDNVAADISNIPHLGCLPSLGEDLARLGTVAKYLPEDDRPGLMSLILVRNAHVSVDVGGRFGVISASMAHFDVAHVSVPSLLAVAARSLEVNRNQIEELVGSSLLASHGDEETPVLVIRLIGGTVEPTITVKLRGLNVEYRVPTIIDLLNLGEDATPQDFEAGLAASVAQFGEQAHVAISGTSAITADSRTIGQDRQKLPVVELYFLDCVVGLNPLGMTSKMGIVLSDSCLKVWLEEKGDAKATWHIKQASILLIDDVALLDPEGKQNVKRHVHRPSDPVSAKIWDMDSVLCAQGFVSISQIRAAIIRVKAIQDEDGQRLIDVEVQDNFLVLETCADSTQTLIGLGNALKPPTPPSKENKFKTEIVPIEDMLASISQDAFGKAEGDYNFDDDFGEPEESDWTEDDLDEDLDIMGALGSQDDGQNTRQLLFDATSSSIMSDRTTTQYANDEVIFSGFSENPSHANSPDMSVENAFFASVPASETPQPEWKSAKMREVVPKEATIKKYPLKIKIRDMHLIWNLFDGYDWQRTRETIGKTVEEIQAKAYERRARMDRRMGYHEEDGLEEEAVSDFLFNSIYIGIPSHQDPRELSQNINQELYGINPSDTESVATTAFTTTTSRMGGPSRPKGKRLKLTRSKHHKITFELSGVNAVVRLLEPGSEETQSLIRVHIRDLDVYDHVPTSTWKRFAMYDEDHGPREMGVPMVDLKVRIVRPVLDVTAEEIVMFVNVLPLRLHVDQDALDFITRFFGFKDDTIKTTSSPSDVPFIQRAEIYDIPVKLDFKPKRVDYAGIRSGRTTEFMNFIILDNASMVMRHAIIYGALGFERFGEMLNDVWMPEIKRHQLPGVLAGLAPVRSLVDVGSGFRHLYEIPIREYKRNGRVVRSIGKGAAAFARTTGTELIKLGAKVAIGTQNMLQGAEGLLVETPEHNRYGVAGPSTVQRPGEWEEIDDSEEDIRHQISLYANQPTGVIQGLRHGYRSLSRDISIARQAIIAVPGEVRESSSATGAAKAVLEKAPIFIFRPAIGATKAIGQTLLGATNSLDPQNLRRMDNKYKPDPKS
Lipid transfer protein required for autophagosome completion and peroxisome degradation. Tethers the edge of the isolation membrane (IM) to the endoplasmic reticulum (ER) and mediates direct lipid transfer from ER to IM for IM expansion. ATG2 binds to the ER exit site (ERES), which is the membrane source for autophagosome formation, using basic residues in its N-terminal region (NR) and to the expanding edge of the IM through its C-terminal region. The latter binding is assisted by an ATG18-PtdIns3P interaction. ATG2 then extracts phospholipids from the membrane source using its NR and transfers them to ATG9 to the IM through its predicted beta-sheet-rich structure for membrane expansion.
Q51ZN8
Q05389
CYCY_RHOCB
Cytochrome c-type cyt cy
Rhodobacter
MLVKTHITKIGVTLFAVALFYGFIYMLSNSLFATRPATAVAVGADGKALLPSVDEAAMPAKAPAAAAPAAETAEAAAPAEPAAPPPPAYVEVDPATITGDAKAGEEKFNKTCKACHKIDGKNAVGPHLNGVIGRATATVEGFKYSTAMKNHVGNWTPERLDIYLVSPKAEVPGTKMSFVGLPEAADRANVIAYLNTLPR
Electron transfer pathways that operates during photosynthesis.
Q05389
P75435
T1SD_MYCPN
Type-1 restriction enzyme specificity subunit MpnII
Mycoplasma
MEAPKFVNNACPIPNLNLSRTEEIELDFPPLQIQQKIATILDTFTELSAELSAELSAELSAELSAELSAELSAELSAELSAELSAELSAELSAELSAELSAELSAELSAELRERKKQYAFYRDYLLNQENIRKIYGANIPFETFQVKDICEIRRGRAITKAYIRNNPGENPVYSAATTNDGELGRIKDCDFDGEYITWTTNGYAGVVFYRNGKFNASQDCGVLKVKNKKICTKFLSFLLKIEAPKFVHNLASRPKLSQKVMAEIELSFPPLEIQEKIADILFAFEKLCNDLVEGIPAEIELRKKQLDYYQNFLFNWVQEQKKNSLSTNLN
The specificity (S) subunit of a type I restriction enzyme; this subunit dictates DNA sequence specificity. The M and S subunits together form a methyltransferase (MTase) that probably methylates A-2 on the top strand and A-3 on the bottom strand of the sequence 5'-GAN(7)TAY-3'. As the bacterial DNA is methylated on this sequence and this is the only type I methylase in the genome, it is probably responsible for all of the methylation on this site in the genome. The R subunit has multiple frameshifts and is probably not expressed in this bacteria.
P75435
Q5PA69
RL24_ANAMM
50S ribosomal protein L24
Anaplasma
MMAKIVSGDDVIVIAGSDKGKIGKVVKILRKGGHVVAKVAGVALCRKSVKPSKDREGGIFSVERFIDISNIALFDSEAGVRTKVGYKFVDGKKVRYLKGSGRVLD
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
Q5PA69
A8AVU5
GPSB_STRGC
Guiding PBP1-shuttling protein
Streptococcus
MASIIFTPKDIFDQDFKTAVRGYSKQEVDEFLDDVIKDYETYSALVKELREENSRLKQELSKRMQEAPNSTASQVHQSFGDTTQTTITNFDILKRLSRLEKEVFGKQIQASELNQL
Divisome component that associates with the complex late in its assembly, after the Z-ring is formed, and is dependent on DivIC and PBP2B for its recruitment to the divisome. Together with EzrA, is a key component of the system that regulates PBP1 localization during cell cycle progression. Its main role could be the removal of PBP1 from the cell pole after pole maturation is completed. Also contributes to the recruitment of PBP1 to the division complex. Not essential for septum formation.
A8AVU5
P76213
CHO_ECOLI
UvrC homolog protein
Escherichia
MVRRLTSPRLEFEAAAIYEYPEHLRSFLNDLPTRPGVYLFHGESDTMPLYIGKSVNIRSRVLSHLRTPDEAAMLRQSRRISWICTAGEIGALLLEARLIKEQQPLFNKRLRRNRQLCALQLNEKRVDVVYAKEVDFSRAPNLFGLFANRRAALQALQTIADEQKLCYGLLGLEPLSRGRACFRSALKRCAGACCGKESHEEHALRLRQSLERLRVVCWPWQGAVALKEQHPEMTQYHIIQNWLWLGAVNSLEEATTLIRTPAGFDHDGYKILCKPLLSGNYEITELDPANDQRAS
Incises the DNA at the 3' side of a lesion during nucleotide excision repair. Incises the DNA farther away from the lesion than UvrC. Not able to incise the 5' site of a lesion. In vitro, the incision activity of Cho is UvrA and UvrB dependent. When a lesion remains because UvrC is not able to induce the 3' incision, Cho incises the DNA. Then UvrC makes the 5' incision. The combined action of Cho and UvrC broadens the substrate range of nucleotide excision repair.
P76213
A6LLA7
NUSB_THEM4
Antitermination factor NusB
Thermosipho
MLKSRHKMREAIFKSLFQWDFNKEEILEEISKEHIVSLEPNLQELAVNYLKGIRENIDVIDEIISKYLKNWTLERLSVTDRNILRLGTYELIYVDDIPIEVTLDEMIELGKTYGTENSGKFVNGVLDKIAKAEAPKEKFEL
Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons.
A6LLA7
Q76NM7
RAB5B_PLAF7
Ras-related protein Rab-5B
Plasmodium (Laverania)
MGCSSSTERLTSTKNINIVTSPAQQQKKNAQDTKVKIVLLGDSGVGKSSIALYLCHGRFSEKHQVTIGAAFLHHNIELKNGATMKLHIWDTGGQERFRSMAPLYYRDAYGAVVVYDSNNVESFDSLKYWINEIKSNGPRNCCIMVVANKKDLPQKLNSEMVMKFCEQENVSFIECSAKTGENITTLFEKLASRIYSRFKEVLYYNNP
Small GTPase which regulates vesicle trafficking between organelles (Probable). May be involved in the trafficking of the N-myristoylated AK2 from the endoplasmic reticulum to the parasitophorous vacuole membrane .
Q76NM7