ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q03073 | MSQPSISKSMTIGESGLAVVFAATAFLCVIAAAKALDAPFAFHAALSAAASVAAVFCIVNRYFERPAALPPAEINGRPNYNMGPIKFSSFMAMFWGIAGFLVGLIIASQLAWPALNFDLPWISFGRLRPLHTSAVIFAFGGNVLIATSFYVVQKSCRVRLAGDLAPWFVVVGYNFFILVAGTGYLLGVTQSKEYAEPEWYADLWLTIVWVVYLLVFLATIIKRKEPHIFVANWFYLAFIVTIAVLHLGNNPALPVSAFGSKSYVAWGGIQDAMFQWWYGHNAVGFFLTAGFLAIMYYFIPKRAERPIYSYRLSIIHFWAL... | Cofactor: Binds 1 copper ion per subunit, denoted as copper B.
Function: Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Co I is the catalytic subunit of the enzyme. Electrons originating in cyto... |
Q05572 | MKHTVEMVVLSVGAFLALVGAGLAQDRLFGAHMWVLFFALLAGTLVLMRRVDFRPAVAGHPGRRREYFDEVVKYGVVATVFWGVVGFLVGVVVALQLAFPELNVEPWFNFGRVRPLHTSAVIFAFGGNALIATSFYVVQRTSRARLFGGDLGWFVFWGYQLFIVLAASGYLLGITQSREYAEPEWYVDLWLTIVWVAYLVAFLGTIMKRKEPHIYVANWFYLAFIVTIAMLHVVNNLAVPVSFLGSKSYSAFSGVQDALTQWWYGHNAVGFFLTAGFLAMMYYFIPKQVNRPVYSYRLSIIHFWAIIFMYIWAGPHHLHY... | Cofactor: Binds 1 copper ion per subunit, denoted as copper B.
Function: Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Co I is the catalytic subunit of the enzyme. Electrons originating in cyto... |
A8HZ17 | MSTSHESHHAPVDGAGGPSTTGHEWDGIQELNNPLPRWWLWTFYATIIWAFGYWVAYPAWPLVSNYTSGVLGWNSRSAVVEQISDLQKLRAASSAKLANVPLEDIEKNPELLSLARAEGKVAFADNCAPCHGAGGGGAKGFPNLNDDDWLWGGTLAQIQQTITHGIRSGDDEGHQGNMLAFGSILSKADISNVADYVRSLSGAAPGDTPAAKKGAEIFAANCATCHGENGKGNQELGSKNLTDGIWLYGGDKATIVQTITNGRGGVMPAWGPRLSPTTIKALTVYVHTLGGGQ | Cofactor: Binds 2 heme C groups per subunit.
Function: C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. FixP subunit is required for transferring electrons from donor cytochrome c via its heme groups to FixO subunit. From there, electrons are shuttled to the catalytic binuclear center of FixN subu... |
Q03075 | MTDHSEFDSVSGKTTTGHEWDGIKELNTPLPRWWVICFYLTIVWAIGYWIVYPAWPLISSNTTGLFGYSSRADVAVELANLEKIRGDKMAALGAASLADVEKDPALLALARAKGKTVFGDNCAPCHGSGGAGAKGFPNLNDDDWLWGGTLDQIMQTIQFGARSGHAKTHEGQMLAFGKDGVLKGDEIVTVANYVRSLSGLPTRKGYDAAKGEKIFVENCVACHGDGGKGNQEMGAPNLTDKIWLYGSDEAALIETISQGRAGVMPAWEGRLDPSTIKAMAVYVHSLGGGK | Cofactor: Binds 2 heme C groups per subunit.
Function: C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. FixP subunit is required for transferring electrons from donor cytochrome c via its heme groups to FixO subunit. From there, electrons are shuttled to the catalytic binuclear center of FixN subu... |
P0AEM2 | MSESVQSNSAVLVHFTLKLDDGTTAESTRNNGKPALFRLGDASLSEGLEQHLLGLKVGDKTTFSLEPDAAFGVPSPDLIQYFSRREFMDAGEPEIGAIMLFTAMDGSEMPGVIREINGDSITVDFNHPLAGQTVHFDIEVLEIDPALEA | Function: PPIases accelerate the folding of proteins. Substrate specificity carried out with 'Suc-Ala-Xaa-Pro-Phe-4-nitroanilide', where Xaa is the amino acid tested, was found to be Phe > Leu >> Ile > Lys = Ala > Trp > His >> Gln (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-pe... |
P21863 | MTDQVLAEQRIGQNTEVTLHFALRLENGDTVDSTFDKAPATFKVGDGNLLPGFEAALFGFKAGDKRTLQILPENAFGQPNPQNVQIIPRSQFQNMDLSEGLLVIFNDAANTELPGVVKAFDDAQVTIDFNHPLAGKTLTFDVEIIDVKAL | Function: PPIases accelerate the folding of proteins.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 16373
Sequence Length: 150
EC: 5.2.1.8
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P44760 | MLKIQKLSIAALMVSAVISGQVFAEDNTFDEKAASYAVGTLMGSQMKDLVDSHKEVIKYDNARILDGLKDALEGKVDVRKDEKIQKTLESIEAKLVAASKAKAESIAKQAKEEGDKFRAEFAKGKDVKTTQSGLMYKIESAGKGDTIKSTDTVKVHYTGKLPNGKVFDSSVERGQPVEFQLDQVIKGWTEGLQLVKKGGKIQFVIAPELGYGEQGAGASIPPNSTLIFDVEVLDVNPKSEK | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 26125
Sequence Length: 241
EC: 5.2.1.8
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P30417 | MLQATCARIARRFVWRNRMPRRLFIGLFLLPLPLFAAPPKDELAYAVGARLGMRLQQEMPGLELSELLLGLRQAYRGEALEIPPERIEQLLLQHENATTETPRTTPAEARFLANEKARFGVRELTGGVLVSELRRGQGNGIGAATQVHVRYRGLLADGQVFDQSESAEWFALDSVIEGWRTALRAMPVGARWRVVIPSAQAYGHEGAGDLIPPDAPLVFEIDLLGFR | Function: PPIases accelerate the folding of proteins.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 25278
Sequence Length: 227
EC: 5.2.1.8
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P40466 | MSVTSREQKFSGKYSSYTAQDRQGLVNAVTCVLSSSSDPVAVSSDYSNSLSIAREVNAYAKIAGCDWTYYVQKLEVTIGRNTDSLNLNAVPGTVVKKNIDIDLGPAKIVSRKHAAIRFNLESGSWELQIFGRNGAKVNFRRIPTGPDSPPTVLQSGCIIDIGGVQMIFILPEQETIISDYCLNHLMPKLLSTYGTNGNNNPLLRNIIEGSTYLREQRLQEEARLQQLDHLHTPLSSSSDVNPIGDPHGDTIMMEEDEEDENYTRGGIRPNTYTSSSNNAVTNGNVPHIENPSDLSLDENRYIKPPQSYASMITQAILSTP... | Function: Transcription factor that regulates the expression of the CLB2 cluster of genes during the G2/M phase of the mitotic cell cycle . The CLB2 cluster of genes includes mitotic regulators such as CLB1, CLB2, CDC5 and CDC20 as well as SWI5 and ACE2, transcription factors required for the subsequent temporal wave o... |
O60129 | MTVRRLESKSEHISDDEERKEQLDYKKQMDVDTDRNIVLNGRLESQIAKLSVPPHEMRVVDDYSNSKNAERHSGEIQAYAKFAGSTWTYYVKKIRIILGREPANPSPKGKNEDLEVIDMNFGPSKVVSRKHAVVEYDLDDQTWNCSVYGRNGIKVDGKLFKNGETVKLTSGSILEVAGLQMMFVLPNAAEQKQTDESTIKEDAIKSEISAAVNDAAEYGDNKKPPYSYSVMIAQAILSSSECMMTLSNIYSWISTHYPYYRTTKSGWQNSIRHNLSLNKAFRKVPRKSGEQGKGMKWSIVPEFREEFIAKTRKTPRKRSP... | Function: Required for promoter sequence element PCB-driven, M-phase-specific transcription. Acts as a transcriptional activator with a role in the regulation of mitosis. Binds, cooperatively with mcm1, the CLB cluster regulatory elements throughout the cell cycle. Regulates the periodic transcription of cdc15 and spo1... |
P41813 | MSSSNFNEMNELNMTQTNYGSTKYTAQHHQGVINAIISSLTAPDQPTTVSLQYSNDKNMATEIQAYAKLSGPNWTYYVKDLEVSIGRNTDPLNSALQENSDGVKNSYRVNIDLGPAKVVSRKHAIIKYNMNIGGWELHILGRNGAKVNFQRTHNGPNNPPIRLSSGTLLDIGGTQMMFILPDSDPVVAPICIEHLMPNLINMFGLEGNNNPLLRDIIKQSNYAKQRQLTSNQQIKGFKLYGSGGNAPFGSGANLGPSEQGIFNNNNNSKNKNGYFTSINPNYTASTTTSNTINPQAASPQGPPNTIIAANFVDSYKSSNA... | Function: Transcription factor that regulates the expression of the CLB2 cluster of genes during the G2/M phase of the mitotic cell cycle . The CLB2 cluster of genes includes mitotic regulators such as CLB1, CLB2, CDC5 and CDC20 as well as SWI5 and ACE2, transcription factors required for the subsequent temporal wave o... |
D4B388 | MLLYYILVALWATVTYAKSFSEDISEMPELSEMSSYLNQTPEAKDVLDQQKNVTLLALENSAFRDFVGQGEGNDNQSSSNSSLLRGIFSYQLVKGLHNSEQITTTPQFSPTELNDAGFTNVSSGQIVQLVEKDGKDYAISGLNDNSTIIKPGVDVENGVIHVIDRPLTLPQSVTATLQAANLTSFQGALQRGNAVSNANDPKDITLFAPRNLGFQRIGTAFENISAEDLGQIANYHIVKGKVLYSPDLTDADHPTYADKDLHISTVDGRSYVNSARVESTNLLVNNGVIHVISDVLNPNNDTAKPVPNADPPPPAFENAN... | Function: May be a cell surface adhesion protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 43547
Sequence Length: 421
Subcellular Location: Cell membrane
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Q30SL9 | MIRNFLLFFMPIYAILFLSGCTANLSDPEIDFEPPAYVEEMPSKEDNKDFTSVGSVFGQGENPLFSDHKAMHVNDIVTVIISENTQSSNSGSKQISESDSLNLGGGAFTSAGTNSAVNSAVSKLNGIANLGFGSTSDSAYKGQGSATKDASFTTTVSARIVKVLQNGNYFISGKREILVDNQKQIIQIGGVIRPYDIDQGNRINSSQMSEAKILYKTQGDVERATDRGWGTKIIQSVWPF | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 25958
Sequence Length: 240
Subcellular Location: Cell outer membrane
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Q2LT21 | MNILIQNRLIFLFLILWLWTGCATKPDFTAGEQPLDLTVRPEALPVRGSIWPGESASNMLFADKKARYINDIVTILINEASQGGNKATTNTSRDSDSAAGIDAFWGLDQSILSRNVNMGSKIKIGGSSSSTLKGTGNTTRGGQLKGTVTARVVRVLDNGNLVIEGRRQLTINEEDQYLIISGIIRPEDITTENCIFSQYIADARIVYAGKGIINDKMRPGWATRIVDWVWPF | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 25534
Sequence Length: 232
Subcellular Location: Cell outer membrane
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Q3A5F4 | MRTWAVLPILLMLVGCVTQRIVEPQPHSAPIAARQVQPEQPQAPGSLWTEGRGSLFRDNKARRVGDIVTVAIYEQASASKQASTATGRSSSMSAGLTNLFGIEGNIGNLNKFIDPTSLIDTSYENAFDGSGSTSRKEDLVATLTAQVIEELPNGNLCIAGGKTVTVNREDQIILLEGIIRPEDISARNVVSSKHILDAKIAYTGKGVISDKQRPGWMTRVLDHIWPF | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 24595
Sequence Length: 227
Subcellular Location: Cell outer membrane
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B5YIX2 | MRKLILISLCIFFLASCSELQEVRDIKNAGMPPKYYPEPPQTQVASEGSLWRNKASLYEDKKARRVNDLVTILINESTSAQKTASTTASRDSSTNYGLDTFFGMNTDFNIHNLPLINGFYKAGNVFSPSVKGSATSDFKGDGDTARTGKITGTITAKVVEVLPNGNLVIESRKEVIVNNEKEILVLRGIIRPDDISQSNTILSQYVADAQIYLVGEGTLGDKQSQGWLVRFLDKIWPF | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 26318
Sequence Length: 238
Subcellular Location: Cell outer membrane
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Q3SIE4 | MKTTRAIAMLGLLLGLAACGTTPSTIVERPTTARPQAPAAVPATNGAIYQAATYRPLFEDRRARHVGDVLTIVINERTRAGKEASSSASKTSAVDASVGGVAKLPLKMFQGLGINAEASAEYEDESALDSSNTFSGNVTVTVIEVLPNGNLVVAGEKQIGLDKGTEYIRLSGVVQPDTIQAGNTVSSAKVADARIEYRSSAKFDKAEVMNWLGRFFLSFIPL | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 23434
Sequence Length: 222
Subcellular Location: Cell outer membrane
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A5F678 | MAAMKRLLASSLLILLSGCSLMQPPIESAETIQGTTTVDAVEGDKSESNSGLTDALRNRTDPVAGDPAWAPIHPKGKPEHYAAETGSLFNLASSSSMYDDSKPRGVGDIITVTLNESTKAAKSADADLNKKNDASMDPLAVGGKDLTIGDYNFSYALKNDNKFSGSAAANQSNSMSGSITVEVIEVLANGNLVIRGEKWLTLNTGDEYIRLSGTIRPDDIDFDNTIASNRISNARIQYSGTGTNQDMQEPGFLARFFNVSL | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 27790
Sequence Length: 261
Subcellular Location: Cell outer membrane
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Q7M7T1 | MSGFLLVTLVAALYSGCSVADPQISFKPPEYVEEMPAREVEESFGNAGSLFGQGDNPLFADRRAMKLNDLVTVIINETASASSSGKKDLSETSSSTMNGPSVTFGGPSQSIGNAVNKLNNFTSFGLSTGNNNSTFAGSGTQQRQESFTTTVSARIIKVMENGNYFIEGGREILINGEKQIMRLTGVIRPYDIGRNNTINSRYIADAKIMYETQGEIKKSTEKGWGTKVLESVWPF | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 25442
Sequence Length: 235
Subcellular Location: Cell outer membrane
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Q3BU05 | MSRLPSLSRLCLAIACSALLGGCVAAGDVRPFAELAPIVPVVAPVAQPTAGAIYAAGPSLNLYGDRRARDVGDLLTVNLVESTTASSTANTSISKKDATTMGAPTLLGAPLTVGGLNVLENSTSGDRSFAGKGNTAQSNRMQGSVTVTVMQRLPNGNLVIQGQKNLRLTQGDELVQVQGIVRAADIAPDNTVPSSKVADARIAYGGRGAIAQSNAMGWLSRFFNSRLSPY | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 23697
Sequence Length: 230
Subcellular Location: Cell outer membrane
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P21184 | MALTVNTNIASLNTQRNLNNSSASLNTSLQRLSTGSRINSAKDDAAGLQIANRLTSQVNGLNVATKNANDGISLAQTAEGALQQSTNILQRMRDLSLQSANGSNSDSERTALNGEVKQLQKELDRISNTTTFGGRKLLDGSFGVASFQVGSAANEIISVGIDEMSAESLNGTYFKADGGGAVTAATASGTVDIAIGITGGSAVNVKVDMKGNETAEQAAAKIAAAVNDANVGIGAFSDGDTISYVSKAGKDGSGAITSAVSGVVIADTGSTGVGTAAGVTPSATAFAKTNDTVAKIDISTAKGAQSAVLVIDEAIKQIDA... | Function: Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.
PTM: Phosphorylated on tyrosine residue(s).
Sequence Mass (Da): 40066
Sequence Length: 394
Subcellular Location: Secreted
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P72151 | MALTVNTNIASLNTQRNLNASSNDLNTSLQRLTTGYRINSAKDDAAGLQISNRLSNQISGLNVATRNANDGISLAQTAEGALQQSTNILQRIRDLALQSANGSNSDADRAALQKEVAAQQAELTRISDTTTFGGRKLLDGSFGTTSFQVGSNAYETIDISLQNASASAIGSYQVGSNGAGTVASVAGTATASGIASGTVNLVGGGQVKNIAIAAGDSAKAIAEKMDGAIPNLSARARTVFTADVSGVTGGSLNFDVTVGSNTVSLAGVTSTQDLADQLNSNSSKLGITASINDKGVLTITSATGENVKFGAQTGTATAGQ... | Function: Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.
PTM: Phosphorylated on tyrosine residue(s).
Sequence Mass (Da): 49242
Sequence Length: 488
Subcellular Location: Secreted
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O67241 | MDKLREYLNLLKERFNALTPVQKALAVGIPLLLLSLGAVALIYLSQENYTVLYTGLSPDDLNAVVTELDKEGVKYKISPDGRTIYVPENVARELRLKLAAKGVPRKGIVGYELFDKSGIVLSRFQQLVNFKRAIEGELAKTIMSLDCVEFARVHIVLPEKSLFIREEEEAKASVFLKLKPGCELTPEQVKAIRNLVSGSVENLKPSQVVVVDDKGRDLTAYLDEEFKTNASQLKVKREFEKSLERKLQKTLEEVFGYGKVKVNVSAELDFSSMKKREELYDPDLTAVVSEQKKKERTTSTRAQGIPGTQANIPPATGRQG... | Function: The M ring may be actively involved in energy transduction.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54450
Sequence Length: 489
Subcellular Location: Cell inner membrane
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P23447 | MNRTLMQMKNKTSEFWKNRSKLQKILMVSALAAIIIIGIIISVFASNSKMAPLYKDLSAEEAGQIKEELDAKKVPNELSNGGTVISVPEDQVDSLKVQMAAEGLPKTGSIDYSFFGQNAGFGLTDNEFDMVKVKATQTELSNLINEMDGIKNSKVMINLPKDAVFVGEEQSAASASIVLQIQPGYTLDQSQINGLYHLVSKSVPNLKEDNIVIMDQNSTYYDKSDSDAGSYADSYSSQQGIKSQVEKDIQKHVQSLLGTMMGQDKVVVSVTADIDFTKENRTEDIVEPVDKENMEGIAVSAEKVSETYQGDGAANGGTAG... | Function: The M ring may be actively involved in energy transduction.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59300
Sequence Length: 536
Subcellular Location: Cell membrane
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Q44912 | MSKFFTNFFVSAKGIFKKASTVQKIALGLIIFFVILALVFLIGFSTKSQSIALFGVEIKDQYLLDRISQRLDRENVKYFLSSDGRIYLDDEKLAKKMRAILVREELVPVHMDPWALFDIDRWTITDFERSINLRRSITRAVEQHIVALDDVDAVSVNLVMPEKALFKESQEPVKASVRITPRPGSDIITNRKKVEGLVKLIQYAIEGLESDNIAIVDNSGTILNDFSNLDGIDRIDLAEKERKLKLKYEAMLRGEIDSALSKVLSVDRFMIARVNVKLDTSKETTESKEYAPIELQSQDPKASYNTRKVSDSTIISSQTQ... | Function: The M ring may be actively involved in energy transduction.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65133
Sequence Length: 569
Subcellular Location: Cell inner membrane
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Q8YDM4 | MAVVWMQQNFQQLIEQLKGTLGKLGARKLIALGLVGAALMGAILYTSIYLGRPSYETLYVGLSRDDVNRMGLALGEAGIPFDVKSDGSSILVPIGKAENARMYLAEKGLPTSNNAGYELFDNMGSLGLTSFMQEITRVRALEGEIARTIQAIRGVKAARVHIVLAEKGSFRRGDQKPSASVVIRAEGGFSAESAQSIRQLVAAAVPSLDASSVTVLDTNGHLLASAGEGANGAALMTASLEQQVASHVDDSIRKALAPYLGLGHFQTSVQAALDTDRRQTKETTYDPESRVERSVRVVRESGDSRNNRNDNATGVEQNIP... | Function: The M ring may be actively involved in energy transduction (By similarity). The flagellum is required to cause a persistent disease in a murine model of infection.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62161
Sequence Length: 580
Subcellular Location: Cell inner membrane
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P54466 | MDPSTLMILAIVAVAIIVLAVFFTFVPVMLWISALAAGVKISIFTLVGMRLRRVIPNRVVNPLIKAHKAGLNVGTNQLESHYLAGGNVDRVVNALIAAQRANIELTFERCAAIDLAGRDVLEAVQMSVNPKVIETPFIAGVAMDGIEVKAKARITVRANIERLVGGAGEETIVARVGEGIVSTIGSSDNHKKVLENPDMISQTVLGKGLDSGTAFEILSIDIADVDIGKNIGAILQTDQAEADKNIAQAKAEERRAMAVAQEQEMRARVEEMRAKVVEAEAEVPLAMAEALREGNIGVMDYMNIKNIDADTEMRDSFGKL... | Function: Found in functional membrane microdomains (FMM) that may be equivalent to eukaryotic membrane rafts. FMMs are highly dynamic and increase in number as cells age. FloA and FloT function is partially redundant; double deletions have marked synthetic phenotypes . Flotillins are thought to be important factors in... |
B8DZW4 | MNLIWGFLILILVLIFLGVFFSFVPLGLWISALAAGVSIRITDLIGMRLRRVPPGVIINSLIKAHKAGLSEVTLDKLEAHYLAGGNVDKVVNALIAAQRAGIPLTFEKAAAIDLAGRDVLEAVQMSVNPKVIETPVVAAVAKDGIELKAKARVTVRANIERLVGGAGEATIIARVGEGIVTTIGSAESYKEVLENPDSISKTVLAKGLDAGTAFEIVSIDIADVDVGNNVGARLKMDQAEADMRIAQAQAESRRALAIAREQEMKALTQEMRARLIEAEKEVPLAIAEALRSGKIGVLDYYTLKNIIADTAMREAISKLG... | Function: Found in functional membrane microdomains (FMM) that may be equivalent to eukaryotic membrane rafts. FMMs are highly dynamic and increase in number as cells age. Flotillins are thought to be important factors in membrane fluidity.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 35210
Seque... |
Q9WZP3 | MADQYHEPVSELTGKDRDFVRALNSLKEEIEAVAWYHQRVVTTKDETVRKILEHNRDEEMEHAAMLLEWLRRNMPGWDEALRTYLFTDKPITEIEEETSGGSENTGGDLGIRKL | Function: Cargo protein of a type 1 encapsulin nanocompartment. A ferritin-like protein that probably stores iron in the encapsulin nanocompartment.
Sequence Mass (Da): 13289
Sequence Length: 114
Domain: The C-terminal 15-30 residues (cargo loading-peptide, CLP, or targeting peptide) are sufficient to target this prote... |
P9WQL7 | MTALNRAVASARVGTEVIRVRGLTFRYPKAAEPAVRGMEFTVGRGEIFGLLGPSGAGKSTTQKLLIGLLRDHGGQATVWDKEPAEWGPDYYERIGVSFELPNHYQKLTGYENLRFFASLYAGATADPMQLLAAVGLADDAHTLVGKYSKGMQMRLPFARSLINDPELLFLDEPTSGLDPVNARKIKDIIVDLKARGRTIFLTTHDMATADELCDRVAFVVDGRIVALDSPTELKIARSRRRVRVEYRGDGGGLETAEFGMDGLADDPAFHSVLRNHHVETIHSREASLDDVFVEVTGRQLT | Function: Part of the ABC transporter complex Rv2686c/Rv2687c/Rv2688c involved in fluoroquinolones export. Confers resistance to ciprofloxacin and, to a lesser extent, norfloxacin, moxifloxacin and sparfloxacin. Probably responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane pro... |
P9WJB2 | MRAISSLAGPRALAAFGRNDIRGTYRDPLLVMLVIAPVIWTTGVALLTPLFTEMLARRYGFDLVGYYPLILTAFLLLTSIIVAGALAAFLVLDDVDAGTMTALRVTPVPLSVFFGYRAATVMVVTTIYVVATMSCSGILEPGLVSSLIPIGLVAGLSAVVTLLLILAVANNKIQGLAMVRALGMLIAGLPCLPWFISSNWNLAFGVLPPYWAAKAFWVASDHGTWWPYLVGGAVYNLAIVWVLFRRFRAKHA | Function: Part of the ABC transporter complex involved in fluoroquinolones export. Probably responsible for the translocation of the substrate across the membrane (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27144
Sequence Length: 252
Subcellular Location: Cell membrane
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P9WJB0 | MTRLVPALRLELTLQVRQKFLHAAVFSGLIWLAVLLPMPVSLRPVAEPYVLVGDIAIIGFFFVGGTVFFEKQERTIGAIVSTPLRFWEYLAAKLTVLLAISLFVAVVVATIVHGLGYHLLPLVAGIVLGTLLMLLVGFSSSLPFASVTDWFLAAVIPLAIMLAPPVVHYSGLWPNPVLYLIPTQGPLLLLGAAFDQVSLAPWQVGYAVVYPIVCAAGLCRAAKALFGRYVVQRSGVL | Function: Part of the ABC transporter complex involved in fluoroquinolones export. Probably responsible for the translocation of the substrate across the membrane (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25576
Sequence Length: 237
Subcellular Location: Cell membrane
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Q6FRT6 | MNYLHNFKDTLFVDLLEVLNIVTIGEEHVNQLNLSGDASLSASSESSNMSFNSGSEENSQEKSVEDLEKQNCEINIHKNSDKEADTKKDPFLVTFNGEDDPLMPYNWSTNKKALIIIQTMLLTCVNYMGSSIYTPGQLEIQNEFHVGHVVGTLNLSLYVLGYGLGPIVFSPLTEISSIGRLPVYMITFFLFTMLQIGCALAPNFAGLVILRFITGVLCSPALSTGGATLGDIVSQNYLALVLGLWSIGAVAAPVLAPLLGASMVVAKDWRWIFWLLFFCCCATMLLLTFFFPETSSDTVLHRKAARIRKLTGDNRYYTEK... | Function: Multidrug transporter that confers resistance to 5-flucytosine (5-FC) and clotrimazole . Confers also resistance to benomyl, but not 4-nitroquinoline-N-oxide, cycloheximide, or fluconazole . Plays direct roles in extrusion of 5-flucytosine and clotrimazole .
Location Topology: Multi-pass membrane protein
Sequ... |
P38124 | MVYTSTYRHTIVVDLLEYLGIVSNLETLQSAREDETRKPENTDKKECKPDYDIECGPNRSCSESSTDSDSSGSQIEKNDPFRVDWNGPSDPENPQNWPLLKKSLVVFQIMLLTCVTYMGSSIYTPGQEYIQEEFHVGHVVATLNLSLYVLGYGLGPIIFSPLSETARYGRLNLYMVTLFFFMIFQVGCATVHNIGGLIVMRFISGILCSPSLATGGGTVADIISPEMVPLVLGMWSAGAVAAPVLAPLLGAAMVDAKNWRFIFWLLMWLSAATFILLAFFFPETQHHNILYRRALKLRKETGDDRYYTEQDKLDREVDAR... | Function: Probable efflux transporter. Confers resistance to the azole derivative fluconazole (FCZ).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61629
Sequence Length: 548
Subcellular Location: Membrane
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Q9HNW1 | MGIPLRIDARSTALVAVGGAVGAVLRYTVAQAIAGPLGTLAANAAGSLALGALAYEAAATDSVLSADAHTLLGTGCLSAFTTYSTFAVQTAGLAPRWMAANVATTYALGFAGVLVGRAIAATARGDRR | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12595
Sequence Length: 128
Subcellular Location: Cell membrane
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Q5FKD1 | MNFLLAGIGASIGAMLRYAITNYGKKHWEWIGNKFSNLPTPTLFINLTGAFILGFIFGIKTNVFIYAIVGTGVLGGYTTFSTMNTELVELYKSKNYRGFIFYALSSYLGGLILVFVGYYLAILF | Function: Fluoride-specific ion channel . Important for reducing fluoride concentration in the cell, thus reducing its toxicity (By similarity).
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13786
Sequence Length: 124
Subcellular Location: Cell membr... |
Q88ZT7 | MKKIIAITGFAMLGGGLREGLSLLVTWPQHFWITCLINIVGAFVLSLITNLLPARLPVSEDIVIGMSVGFVGSFTTFSTFTFETLQSFQSGHSVLALSYVAASLGLGLLAGLAGNFLSTYWLPKEEF | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13647
Sequence Length: 127
Subcellular Location: Cell membrane
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Q38ZE4 | MTILLVGLGAALGAILRYQLTRIGNHIASEFPLMTFLINLTGSFCLGWLTGSQLSQPVTLFLGVGVLGGYTTFSTLNSELSQLWFRRRYHIFFGYWLLTYGLGLLVAAAGFYAGL | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12601
Sequence Length: 115
Subcellular Location: Cell membrane
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Q6AHI4 | MSRRSSFPVHLHGRSMLLVFVGGALGTAARALLSAAAPTVAVISVITFVINVIGAFVLGWLLESLALRGPDEGRRRDVRLFAGTGVLGGFTTYSAFAVDTDGLIVASNVGGGILYAAATIAIGAAAYLAGIALGAAIGCRRGVSA | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14588
Sequence Length: 145
Subcellular Location: Cell membrane
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Q1WS51 | MIEVQNVKLGTLISVFFFGMIGGTLRYLLSLKLASTGTILVNLIGSFCLAFLTYYVIERQKLPAWLSTGLGTGMVGAFTTFSTFTVDILGLSTFTDATFYLLISVVGGFLLAYTGMILGIKLGKVGDRR | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13940
Sequence Length: 129
Subcellular Location: Cell membrane
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Q8Y5I0 | MYFLYVGVFGALGGMCRYAMNLWLGGGDFPSATLAVNLIGCFLLAFLMRFLAEKSRVSLVLLNGIGTGFIGAFTTFSAFSVDTIQLVQSGAWLFAVSYVLASFIGGLIMVKFGRMLSNKLLNRGEHRVG | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13952
Sequence Length: 129
Subcellular Location: Cell membrane
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Q8TIQ4 | MPSQDKEIDKIFLIGAGGFLGAVCRFLLCELVEGQLGILSVNVIGSFMLGMIMYDTEYLGFIGPKGKIAFGTGFMGAFTTFSTFAVQSFSLPFIPALGNISANIFLTLTGVFFGRSVIKALSSREI | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13496
Sequence Length: 126
Subcellular Location: Cell membrane
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Q2FLB7 | MEHLILVGIGGAVGAMLRFELSKLRPVRSIPLGTALVNIIGSSLFGCVVFSRSPGDIFYLVDVGILGGFTTFSTFSFETFRMFEEQDYQTMVLNISINLIGSLIGVLLSFILVTLILTGG | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12952
Sequence Length: 120
Subcellular Location: Cell membrane
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Q2RL34 | MAWLYVGCGGIAGTLARFLLSRWLGNRVRGTWPLGTLFVNLSGAFLLGLLLALPQGRLPANVTLALGTGFVGAYTTFSTFTYETVTMIGDGEGKRALAYSLGSILGGLLLAWLGWLAAGSLF | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12831
Sequence Length: 122
Subcellular Location: Cell membrane
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P63865 | MTASTALTVAIWIGVMLIGGIGSVLRFLVDRSVARRLARTFPYGTLTVNITGAALLGFLAGLALPKDAALLAGTGFVGAYTTFSTWMLETQRLGEDRQMVSALANIVVSVVLGLAAALLGQWIAQI | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13167
Sequence Length: 126
Subcellular Location: Cell membrane
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P61393 | MTTVAVWVGVALIGGVGSVLRFVVDGAVARRASRPFPLGTLVVNLSGAALLGFLGGLALSREAALLAGTAFVGAYTTFSTWMLETQRLGEERQLRAALANIVVSVVLGGAAAFIGQQLAQLV | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12484
Sequence Length: 122
Subcellular Location: Cell membrane
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Q8FMR6 | MQVSIPVCYPCPSFPQTRPFAGDGRKFGRVDSGFMPKLWEGLSVGAGAAVGACARLALTMQFGEGLWPILAINMLGSFLMGRYRPGPFWGTGVLGGFTTFSAFAVVLVDVPLPHAVAYLTVTVVSCVAAWLMGNRWSA | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14676
Sequence Length: 138
Subcellular Location: Cell membrane
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A9KG69 | MNVLLIFLGCGAGGVARYGVSNLMYLLMGKQFPIGTLIVNITGSLLMGILFIFILERLSGNIQLWRSLLLIGFLGGYTTFSSFSIETFNLIEAGHYFGAALNVLLSVALCIAGAWLGVLIGRQL | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13334
Sequence Length: 124
Subcellular Location: Cell inner membrane
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Q8VM97 | MGPLGFVAVGVGAAAGAWLRWGFAVLWNAINPALPYGTLAANLLGGYLVGLAVGFFDTHAGLPPEWRLLAITGFLGGLTTFSTFSSEVVANLIAGDYGWAGLHLLLHLGGSLLLTAFGLWTYRLLA | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13116
Sequence Length: 126
Subcellular Location: Cell inner membrane
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Q11UI4 | MLHFILVLVGGAIGSGSRYLLSLHITRTYPGTFPYSTFAVNIIGCLLIGIIYGLAERFQLAVHWRLFLATGLCGGFTTFSAFAYENILLLQNGNYTAFTVNTLGSCMFGFTAVFLGVMLTKISI | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13503
Sequence Length: 124
Subcellular Location: Cell inner membrane
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Q3Z6F1 | MGEILLLAAGGALGAVSRYGLNNLTVKLLGDSFPYGTLIVNCLGCFVLGFLMQWGFSSDSHNTHLKLMLTAGFLGAFTTFSTFSYETLDCFKNGDYFNGFSNILANVLLGLLMVFIGAYLGSLLKQNSGT | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13915
Sequence Length: 130
Subcellular Location: Cell membrane
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Q9RXX0 | MSFPLWLWLALGGAVGAVCRQAAVLLLAPLVARTGFPAAVLLINVLGSFLLGLTLALTGRGVWPEAVRMTFGTGVLGAFTTFSTFSTELDGLLLRGQGGLALAYAALSVGLGLTAAVAGRVLGARL | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12784
Sequence Length: 126
Subcellular Location: Cell membrane
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Q6AP26 | MDPVMGIIAVALGGAVGSLARYAIALGTQKIAHAFPFGTFIANLAGCLFIGLLWSFFEKIHISHTFRLFLFTGLLGGLTTFSTFSRETYGFFETGEYWQGFGYLFLSISLGLAMVAVGFFISHKFLLR | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14037
Sequence Length: 128
Subcellular Location: Cell inner membrane
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Q72BN6 | MHRFVLVATGGIFGSLARYVLSGVAQKLTTSSFPYGTVLVNLLGSLLFGLVWGILENRITFAPEARLLLLTGFMGSLTTFSTLTYEGMVLLQSHMWLQAALYIVGQTVAGIMLVWFGAGLGRLV | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13401
Sequence Length: 124
Subcellular Location: Cell inner membrane
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Q01QP2 | MKYLLIALGGGTGSLARYLLGTAITSRVGARFPIGTMVVNVSGCFAIGLAMTLLTERLQPHPYWRLALVVGFLGGYTTFSSFEWETYAAVREGGFWIGLANVLGSVTLGYAAVWFGALLARR | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13097
Sequence Length: 122
Subcellular Location: Cell inner membrane
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A9GIP6 | MERWFWIGLGGAAGTLARYGLSTWCQQRFGAEFPYGTLAVNVIGSFLLGAIGEIAATTELLSPTLRLSLSTGVMGGFTTYSSFNNETIRLIEYKSWAAGLANIAITLVVCLLAGVLGMVVARRLIAG | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13495
Sequence Length: 127
Subcellular Location: Cell inner membrane
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Q1GRB2 | MNSLFPVMVGGAVGAGARHLVGQAMLARFGPGFPWWTLSVNIVGSLAMGLLIGLLARSGTGGETTRLFVGVGMLGGFTTFSSFSMEFWLLFERGQSVQAGLYVVASVVGALLACGAGMILIRQLPA | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13024
Sequence Length: 126
Subcellular Location: Cell inner membrane
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Q30TB5 | MSWQTILAIGSGGFIGAVLRAYFNGIISHKMPHDIPFGTLGVNLVGSFIMGILIAYFMYSTIFSLHVKSFLSTGVLGALTTYSTFAIESFLLLNSGHIALALANISLNAFGSILMAGGGFYIIKLSLRA | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13713
Sequence Length: 129
Subcellular Location: Cell inner membrane
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A6Q9S3 | MQPYLLLAVGTGGFVGAILRFLISGWVQRLSPTLFPVGTLSVNVLGSFIIGFLALYFESVVAPHQKALVITGMLGALTTFSTFSLETVTMLQGGLWGRVVTNITLNVFLCVVATMLGMMLFKRLYG | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13593
Sequence Length: 126
Subcellular Location: Cell inner membrane
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B2V9L9 | MEKYLVIAVGGSIGAILRYLTGVYSAKFFGTWLPYGTLIVNVVGSFILSFFMILFLEKLSLDPLWRLFVAVGFCGSYTTLSSITYETLSIVMDGDYVRALLNIALNFGLSFLSAFAGIVLARML | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13646
Sequence Length: 124
Subcellular Location: Cell inner membrane
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Q00045 | MNTLQKGFTLIELMIVIAIVGILAAVALPAYQDYTARAQVSEAILLAEGQKSAVTEYYLNHGIWPENNPAGVASPASDIKGKYVQSVTVANGVVTAQMKSDGVNKEIKNKKLSLWARREAGSVKWFCGQPVTRDNAGTDAVTADTTGKDKEIDTKHLPSTCRCFQIGSVKWFCGQPVTRDNAGTDAVTADTTGKDKEIDTKHLPSTCRDKSSAE | Function: Major component of the type IV pilus (T4P) that plays a role in cellular adherence, microcolony formation, resistance to neutrophil mediated killing, twitching motility as well as transformation. Mediates the attachment and the formation of bacterial microcolonies on host epithelial cells. Mechanistically, pi... |
Q50228 | MKTIVKLDLDKKPWEQDGQIHNRWHPDLPMIAMVKPGDEFRVECMDWTGGQIGNNDSANDVRDVDLTQVHYLSGPIGVEGAEPGDLMVVDILDVGTFDDSQWGFNGLFAKENGGGFLTDHFPEASKTIWDFHGVYTTSRHVPKVRYAGIMHPGLIGCLPSKELLDTWNKREGDLIATDPDRVPPLACPPTSQSAVMGRLSGDAAKKAAAEGARTVPPRDHGGNCDIKNLTKGSRVYFPVYVKDGGLSMGDLHFSQGDGEITFCGAIEMAGYLDIKVGLIKDGVKKYGIKNPVFQPSPITPTYRDYMIFEGISVDEAGKQH... | Function: Hydrolyzes formamide with the production of ammonia which can be used as a source of nitrogen for growth. Also acts, more slowly, on acetamide, propanamide and butanamide.
Catalytic Activity: formamide + H2O = formate + NH4(+)
Sequence Mass (Da): 44466
Sequence Length: 407
EC: 3.5.1.49
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Q9URY7 | MAPRTIVKVDLNKPAWEQPNLHNRWHPDIPFAESIDEGETVKIECLDWTGGQIKNDDSAEDIKNVDLTRIHYLSGPFEIKGAEPGDVLVVEIQDVQPLENQPWGYSGIFAKENGGGFLDEHYPKAAKAVFDFEGIFCSSRHIPGVRFPGLIHPGIIGTAPSKEILAEWNRREGALVAENPHSTHVMAQLPNASYAFAGILADEKLSATVASEGARTIPGRPENGGNCDIKNLSRGSKVFLPVHVPGAKLSIGDLHFSQGDGEISFCGAIEMAGSITIKCKILKNGISDLAMKSPMYLPGPVEPHFSPSRYLTFEGFSVDE... | Function: Hydrolyzes formamide with the production of ammonia which can be used as a source of nitrogen for growth. May also act on acetamide, propanamide and butanamide (By similarity).
Catalytic Activity: formamide + H2O = formate + NH4(+)
Sequence Mass (Da): 44793
Sequence Length: 410
Subcellular Location: Cytoplasm... |
Q48943 | MTEGVLINENEVESKLEAVIKPGSFTGENAGEMAEVILIPKKAIDIKLEADVITPDSFAGKSAEEIGKLSVWQGPKTYPLSEFFEVTGNGGSSAAETLIRIKGDAMRIKRIGESMSAGKIEIEGSAGMHVGTGMKGGELVVYGDADSWAGMEMTGGLLHIKGNAGDHVGCAYRGKWHGMKGGRIVIEGSARHQLGGGMDGGEILVEGDVKSFCGIRQNGGLIFVKGSALRGVGAEMAGGTIVIGGKIERFSPGFEFVSMENSITSGEVELIGEFKKFTGDYAISKRAKGALYVVADTNPEL | Function: Catalyzes the reversible oxidation of CO(2) and methanofuran (MFR) to N-formylmethanofuran (CHO-MFR). Can use N-furfurylformamide, formamide, N-methylformamide, and formate as substrates. This enzyme is oxygen-labile.
Catalytic Activity: H2O + N-formylmethanofuran + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + H(... |
O27002 | MGFVLVPKSDFQIPLEADTIRPDLFEGLDLDEIRSLQVYEGNIKRPLGEFFEIAETPHADQLIRIDGDVSRVKYIGSGMKSGKIIINGDVGLQLGCEMKGGEIEVNGNVSSWIGMEMHGGTIKINGNAGDYVGCAYRGEWRGMKGGKIIIQGNAGNNIGGGMMAGEIYIGGDAGNFCGIRMNGGEITVRGDAGRAPGAEMVSGIIKIHGRISSLLPGFKEISTFKEDGSLMILFKGDLSEKNPEGNLYINYNKNLHILENETDEGRVITKKGIKVIYNSGSTIREGQIIKGGNKLTDDYIDECARCCISPEDYKLLGEPE... | Function: Catalyzes the reversible oxidation of CO(2) and methanofuran (MFR) to N-formylmethanofuran (CHO-MFR). Can only oxidize formylmethanofuran. This enzyme is oxygen-labile.
Catalytic Activity: H2O + N-formylmethanofuran + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + H(+) + methanofuran + 2 reduced [2Fe-2S]-[ferredoxi... |
P10552 | MGIALMFLLALYQMQSAIHSEIIDTPNYAGNSLQDADSEVSPSQDNDLVDALLGNDQTERAELEFRHPISVIGIDYSKNAVVLHFQKHGRKPRYKYDPELEAKRRSVQDNFMHFGKRQAEQLPPEGSYAGSDELEGMAKRAAMDRYGRDPKQDFMRFGRDPKQDFMRFGRDPKQDFMRFGRDPKQDFMRFGRDPKQDFMRFGRTPAEDFMRFGRTPAEDFMRFGRSDNFMRFGRSPHEELRSPKQDFMRFGRPDNFMRFGRSAPQDFVRSGKMDSNFIRFGKSLKPAAPESKPVKSNQGNPGERSPVDKAMTELFKKQEL... | Function: In insects, FMRFamide and related peptides have modulatory actions at skeletal neuromuscular junctions, and peptides that are immunologically related to FMRFamide are released into the circulation from neurohemal organs.
PTM: This precursor includes 13 peptides that have FMRF or related sequences at their C-t... |
Q08325 | MLAAAKYRNLDPAFVERLAQEAAERFRDRGQAVKYAKRKLHQAFGAFVAGTPAQAVAACVAKIAAGAEPKEAGREAMRAHASSAERVDWLEPFYERVAQWCGPASSVIDLACGLNPLAVPWMALAPGATYACYDVDRTMAEALRALGTVYPVRVNAAAVDLVAAVPAAGVDVALVLKTLTTVEQQRGGRRVAEYRRELTAVQHHSDGARSLSGRRGYADDPDAIVQRAVHGTGYEVVDEAAFGTEALYHLVPLAGTAGRPAPAEGAAEPGATRPVVDVPATARPDADRVDPTG | Function: Specifically methylates the N(7) position of guanine 1405 in 16S rRNA (By similarity). Confers resistance to aminoglycosides.
Catalytic Activity: guanosine(1405) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(1405) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30922
Sequence Length... |
P50264 | MNTVSPAKKKVIIIGAGIAGLKAASTLHQNGIQDCLVLEARDRVGGRLQTVTGYQGRKYDIGASWHHDTLTNPLFLEEAQLSLNDGRTRFVFDDDNFIYIDEERGRVDHDKELLLEIVDNEMSKFAELEFHQHLGVSDCSFFQLVMKYLLQRRQFLTNDQIRYLPQLCRYLELWHGLDWKLLSAKDTYFGHQGRNAFALNYDSVVQRIAQSFPQNWLKLSCEVKSITREPSKNVTVNCEDGTVYNADYVIITVPQSVLNLSVQPEKNLRGRIEFQPPLKPVIQDAFDKIHFGALGKVIFEFEECCWSNESSKIVTLANST... | Cofactor: Binds 1 FAD per subunit.
Function: Involved in the production of beta-alanine, a precursor of pantothenic acid. Multicopy suppressor of fenpropimorph resistance.
Catalytic Activity: H2O + O2 + spermine = 3-aminopropanal + H2O2 + spermidine
Sequence Mass (Da): 57806
Sequence Length: 508
EC: 1.5.3.17
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P15488 | MLKIKYLLIGLSLSAMSSYSLAAAGPTLTKELALNVLSPAALDATWAPQDNLTLSNTGVSNTLVGVLTLSNTSIDTVSIASTNVSDTSKNGTVTFAHETNNSASFATTISTDNANITLDKNAGNTIVKTTNGSQLPTNLPLKFITTEGNEHLVSGNYRANITITSTIK | Function: Fimbriae (also called pili), polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, enable bacteria to colonize the epithelium of specific host organs.
PTM: A longer minor form, starting at amino acid 15, has been detected by amino acid s... |
Q2FZK3 | MKFNKVKLVIHACVLLFIIISIALIFHRLQTKTHSIDPIHKETKLSDNEKYLVDRNKEKVAPSKLKEVYNSKDPKYKKIDKYLQSSLFNGSVAIYENGKLKMSKGYGYQDFEKGIKNTPNTMFLIGSAQKFSTGLLLKQLEEEHKININDPVSKYLPWFKTSKPIPLKDLMLHQSGLYKYKSSKDYKNLDQAVKAIQKRGIDPKKYKKHMYNDGNYLVLAKVIEEVTGKSYAENYYTKIGDPLKLQHTAFYDEQPFKKYLAKGYAYNSTGLSFLRPNILDQYYGAGNLYMTPTDMGKLITQIQQYKLFSPKITNPLLHEF... | Function: Catalyzes the liberation of D-alanyl moieties present on wall teichoic acid (WTA) and lipoteichoic acid (LTA) (By similarity). Affects the methicillin resistance level and autolysis in the presence of Triton X-100 as well as the cell wall structure .
Catalytic Activity: [(4-D-Ala)-(2-GlcNAc)-Rib-ol-P]n-[Gro-P... |
B5Y7I0 | MKIAFFSSGTFGLPVLEELKKENHEIVLITKVDAPSGRGLKLQPSPPAVVAEALQIPIVKVNSLKNDFIEWYFSQGFDVAIVVDFGFYIPKQLFQADKPVMVNIHPSLLPKYRGPNPIRRAICSGELETGVTLIKISEKMDEGDIYLQERVLIDPDDDYVSLTPKLQHVSMELLKKFFLELKQGNLRAFPQLGDPSYAPKFTPDELWIDWQKPAHDIQNQVRALADVGAKTTLGSKLVKIFKVRISGMEDSLPPGHYVAEKESLYVGTGQGSLEILSLQQEGRKKQDAASFVKGLREKEGVFGG | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
Q4JVI0 | MKIVFAGTPEPAAVALEHLIADERIEVVAVVTQPDAKRGRGRSLRPSKVAEVAEEAAIPTYKWPSLKAGTESGDEARAVLGDLAAQGVTAAAVVAYGNLIPKDILDVFEHGWVNLHYSLLPRWRGAAPVQAALAAGDETTGASIFRIEEGLDTGPVAAQLTQKIGLEDTADDLLASLTYAGRELLADTLVAMDEGKAELSGQDDAQATHAPKIHPADAQIDWSQPAEVIQRVARAHTPAPGAWTLLDGQRYKIGMLLPSDPADVAELGPGEVVASPKKVFVGTGTGPLEITRIQPPGKKMMEAAAWARGQQELLAGRPTF... | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
Q6A8H1 | MRLLFAGTPDVAVPTLTALVADPRHEVAAVLTRPDAAVGRHRTPRPCPVAKAAEELGIPAIKATSVKSGEGHDAITSLDADVAVVVAYGGLIPADLLAVPRHGWINLHFSLLPRWRGAAPIQRAIMAGDEETGACVFQLVESLDAGPVYRTMTVPIGPMTTAGELLDELAHTATPLVIEALEDIEAGVEPTPQSVEGVTIAPQIHPDDVRVTVTAAAQEIDNLVRGVSPTPGAWAELDGKRFKILRTRCLEAGDGVPSTVATAQPGQLVATRKQLFLGTGSQPLELLQVQAFGKRAMSGADWARGADIDAGTRLR | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
B2A2K2 | MRTIFMGTPDFSVPFIEAIARSTHNLNLVVTQPDRRKGRGKELQPPPAKRKAEELGIDVFQPESIHNNYAYQILSDIEPHLIVTAAYGQILPRKILDLPRIKAINVHASLLPEYRGAAPIHRAVMDGKEQTGVTIMEMCDKMDAGDILNYESVDIGKTDTTGDVYKQIITVGPQLLIETMDLLEKNQVTPLKQDENQVSYAPKLKKEDEYLDFSKYTNTEVFNRVRGLNPWPGAFTKFEGKRLKIWETKVHNSSSFNSNSKPGEIIEINQQGPVVKCCQGSVILTKIQPSGKKAMTGEQFIRGYDIKSGIQLE | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
Q9K1K6 | MKVIFAGTPDFAAAALRAVAAAGFEIPLVLTQPDRPKGRGMQLTAPPVKQAALELGLRVEQPEKLRNNAEALQMLKEVEADVMVVAAYGLILPQEVLDTPKHGCLNIHASLLPRWRGAAPIQRAIEAGDAETGVCIMQMDIGLDTGDVVSEHRYAIQPTDTANEVHDALMEIGAAAVVADLQQLQSKGRLNAVKQPEEGVTYAQKLSKEEARIDWSKSAAVIERKIRAFNPVPAAWVEYQGKPMKIRRAEVVAQQGAAGEVLSCSADGLVVACGENALKITELQPAGGRRMNIAAFAAGRHIEAGAKL | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
Q820J7 | MRIIFAGTPDFAARALEELQKAGLDIVLTLTQPDRPAGRGMKMQASPVKILAQQYDIPLLQPETLKSSDIQAQLATFKPDVMIVAAYGLLLPEAVLRIPRHGCINIHASLLPRWRGAAPIQRALLEGDTETGISIMQMNQGLDTGAVLLKRSLPIEPYDTTATLHDKLADLGGKCIVEALTLLDQGRLISEPQNEVDACYAAKIRKIEAEIDWTCDAAYIDRMIRTFDPHPGAFTHLQGNTIKLWQARIVSHVNHNSSHQAGKIITVDPDGIVVACGRDALSIDILQKAGGKKLTAAQFLAGHPLHPGESFHKATQDNQG... | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
Q3J6T9 | MAAPPHILFAGTPVFAAIILRRLLEAKYHIGAVYTQPDRPSGRGRRPTPSPVKDIAITHQLPLYQPATLKDKGSQAQLAALAPDLMVVAAYGLILPATVLQIPPLGCINVHASLLPRWRGAAPIQRALLAGDKVTGISIMQMDAGLDTGPVVHTARYPIHPKDTAATVHDQLAELGAEALLQCLPSLLEKKANIATLQDESQACYAPKIRKEEAWLDWSQPAVLLERQVRAFNPWPVAQTQIGGKTLRVWSAAALAQTANALPGTLLAVHKTGIDVATGNGTLRLLEVQLAGKRVMTVQDYLNAHTLTPGIVLVKNPGKA... | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
A6Q4C9 | MRIVFMGTPDYATTILEGLLEKFEVVGVFTQPDKPVGRKQVVTPPHVKKFLIEKNVDIPIFQPSTLKSEEVYEQLHTLAPDFIVVAAYGQILPKEILQLAPCINLHASLLPKYRGASPIQHALLNGDTVTGVTAMLMDEGLDTGDILAYDVIDIQNSDNAITLFEKLSHLAKELTPKVLQSFENIAPIAQHDVDASYCKKIRKQDGQIRFSDAKVIWNKYRAFIVWPGIFLENGLKLKEIDLVETDNTHEEGKILEISDAGVVVGCRRGSICIKSVQPPSKKAMEAVAYLRGKRLKVGDTFF | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
Q827P7 | MKLVFAGTPEVAVPALDALIASGRHEVAAVVTRPDAPAGRGRRLVASPVAQRAEEAGIEVLKPVKPRDEEFLARLREIAPDCCPVVAYGALLPRVALDIPAHGWVNLHFSLLPAWRGAAPVQHSIMAGDEITGASTFLIEEGLDSGPVFGTVTEEIRPTDTSGDLLTRLAFAGSGLLVATMDGVEEGKLKAVPQPADGITLAPKITVENAHVDWSTPALRVDRVVRGCTPAPGAWTVFRGERLKLIQVVPVPERTDLAPGALSVGKNNVYVGTGSYAVELLWVQAQGKKPMRAADWARGVRITDGEPLGA | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
O29370 | MRVALLGGTGNLGKGLALRLATLGHEIVVGSRREEKAEAKAAEYRRIAGDASITGMKNEDAAEACDIAVLTIPWEHAIDTARDLKNILREKIVVSPLVPVSRGAKGFTYSSERSAAEIVAEVLESEKVVSALHTIPAARFANLDEKFDWDVPVCGDDDESKKVVMSLISEIDGLRPLDAGPLSNSRLVESLTPLILNIMRFNGMGELGIKFL | Function: Catalyzes the reversible reduction of NADP(+) by F420H(2). In this reaction the proS hydrogen at C5 of F420 is transferred into the proS position at C4 of NADPH.
Catalytic Activity: NADP(+) + reduced coenzyme F420-(gamma-L-Glu)(n) = 2 H(+) + NADPH + oxidized coenzyme F420-(gamma-L-Glu)(n)
Sequence Mass (Da): ... |
Q58896 | MKIAILGGTGDQGFGLALRLAKNNKIIIGSRKKEKAEEAAKKAKEILKQRGIEADIIGLENKDAAKEGDVVILSLPYEYTLSTIKQLKEELKGKIVVSIGVPLATAIGDKPTRLLFPPDGSVAEMVQNVLKESKVVSAFQNVCHAVLEDLDNPVDCDILVCGNDEEAKKVVIDLANQIDGVRAIDCGNLEKSRIIEAITPLLIGLNIKYKSKGTGIRITNLEI | Function: Catalyzes the reduction of NADP(+) with F420H(2) via hydride transfer, and the reverse reaction, i.e. the reduction of F420 with NADPH. Probably functions in the regeneration of NADPH required in biosynthetic reactions.
Catalytic Activity: NADP(+) + reduced coenzyme F420-(gamma-L-Glu)(n) = 2 H(+) + NADPH + ox... |
P80951 | MKVGIMGGTGNIGEGLARRIXIGGKYDVMIKGRDKA | Function: Catalyzes the reduction of NADP(+) with F420H(2) via hydride transfer, and the reverse reaction, i.e. the reduction of F420 with NADPH. In M.organophilum, an alcohol-fermenting methanogen containing an NADP-dependent alcohol dehydrogenase, is probably involved in the regeneration of F420H(2) required for CO(2... |
D9PVP5 | MKIAVLGGTGDQGLGLALRLALAGEEVIIGSRDAEKAVSAAQKVLEIAERDDLKVKGATNAEAAEEAEVAILTVPLQAQMATLGSVKEAIKGKVLIDATVPIDSCLGGSAVRYIDLWDGSAAERAARFLEDQGTRVAAAFNNISASALLDITGPVDCDCLIASDHRDALDLASELAEKIDGVRAIDCGGLENARVIEKITPLLINLNIKNRIRNAGIRITNLPE | Function: Catalyzes the reduction of NADP(+) with F420H(2) via hydride transfer, and the reverse reaction, i.e. the reduction of F420 with NADPH. Probably functions in the regeneration of NADPH required in biosynthetic reactions.
Catalytic Activity: NADP(+) + reduced coenzyme F420-(gamma-L-Glu)(n) = 2 H(+) + NADPH + ox... |
Q9FKW6 | MAAAISAAVSLPSSKSSSLLTKISSVSPQRIFLKKSTVCYRRVVSVKAQVTTDTTEAPPVKVVKESKKQEEGIVVNKFKPKNPYTGRCLLNTKITGDDAPGETWHIVFTTEGEVPYREGQSIGVIPEGIDKNGKPHKLRLYSIASSAIGDFGDSKTVSLCVKRLVYTNDGGEIVKGVCSNFLCDLKPGDEAKITGPVGKEMLMPKDPNATIIMLGTGTGIAPFRSFLWKMFFEEHEDYKFNGLAWLFLGVPTSSSLLYKEEFEKMKEKNPDNFRLDFAVSREQTNEKGEKMYIQTRMAEYAEELWELLKKDNTFVYMCGL... | Function: Plays a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing power.
PTM: May form interchain disulfide bonds with LIR1.
Location Topology: Peripheral membrane protein
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[fe... |
Q9M0V6 | MALSTTPSQMSVALPTRIDGSSRSMIKVQSISFTDKSWGPPLLRLDSKSRSLGVKKRSTICMSLQQSSKSKVLVTPLELEDPKETPLNLFRPKEPYTATIVSVERIVGPQAPGETCHIVIDHDGNVPYWEGQSYGVIPPGENPKKPGAPHNVRLYSIASTRYGDSFDGKTASLCVRRAIYYDPETGKEDPSKAGVCSNFLCNAKPGDKVKITGPSGKVMLLPEDDPKATHIMIATGTGVAPYRGYLRRMFMENVPNFKFDGLAWLFLGVANSDSLLYDEEFAGYRKDYPENFRYDKALSREEKNKKGGKMYVQDKIEEYS... | Function: Maintains the supply of reduced ferredoxin under non-photosynthetic conditions.
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 42396
Sequence Length: 378
Subcellular Location: Plastid
EC: 1.18.1.2
|
Q9S9P8 | MSHSAVSQAGAVSVSIENQRSLRRSVFKQNNSISFNSKSWSSSLALNQKTTSIRDGKRYPSTTICMSVQQTSSSKVTVSPIELEDPKDPPLNLYKPKESYTAKIVSVERVVGPKAPGETCHIVIDHDGNLPYWEGQSYGVIPPGENPKKPGAPHNVRLYSIASTRYGDFFDGKTASLCVRRAVYYDPETGKEDPSKNGVCSNFLCDSKPGDKIQITGPSGKVMLLPESDPNATHIMIATGTGVAPYRGYLRRMFMENVPNKTFSGLAWLFLGVANTDSLLYDEEFTKYLKDHPDNFRFDKALSREEKNKKGGKMYVQDKI... | Function: Maintains the supply of reduced ferredoxin under non-photosynthetic conditions.
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 42789
Sequence Length: 382
Subcellular Location: Plastid
EC: 1.18.1.2
|
P46908 | MNFLSVRPSDSDLISSDLYELLESISTKRKMEKHTYLFREGMDAEELYLIQSGLIEIGKLTSDGKDLTLRICQKHDIVGELTLFTEEPRYMLSAKVLEDGEVLVINKNKLEKELIQNGALTFEFMKWMSTHLRKIQSKIRDLLLHGKKGALYSTLIRLSNSYGVERSDGILINIVLTNQDLAKFCAAARESVNRMLGDLRKKGVISIDESGKIILHKRDYLRCEIECENCPLEICNID | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: It is involved in the activation of genes necessary for anaerobic respiration.
Sequence Mass (Da): 27218
Sequence Length: 238
Domain: The cysteine cluster which is probably involved in the coordination of the [4Fe-4S] cluster is located at the C-terminal part of... |
Q46158 | CEIPFETLDDLSGKMPNLRQQMMRLMSGEIKGDQDMILLLSKKNAEERLDVFIYNLSRRFAQRGFSPREFRLTMTRGDIGNYLGLTVETISR | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: It is involved in the activation of genes necessary for anaerobic respiration. It probably also activates genes involved in the production of virulence factors.
Sequence Mass (Da): 10704
Sequence Length: 92
Subcellular Location: Cytoplasm
|
Q54CY5 | MNKILLKRQILYNLPKYFKNNIPYTITINKSNQFINNNCKNNNNNFRKLNFTTTTTTTTTAPITNNKPKSNMLYSPKDRSYEEAVNALLTLQSNQTVIISWTKERRDNKEESAKFLMEEMRNYCKTLSIDLERESIIHVAGTKGKGSTCAITESIIREQGFSTGLFTSPHLISPRERIRINGEMISKEMFSQYFWNCWDLLIKDYQTQLPNFFRYLTLMALKIFQDEAIQCTILEVGIGGRMDSTNVFPKPMVTGISALGYDHQNLLGNTLAEIALEKAGIMKVGIPIFTVSSQLPEAINVLIDHSNKVKSPLSIVPSID... | Function: Conversion of folates to polyglutamate derivatives.
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + ATP + L-glutamate = (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP + H(+) + phosphate
Sequence Mass (Da): 70637
Sequence Length: 626
Pathway: Cofactor biosynthesis; tetrahydrofolylpol... |
P08192 | MIIKRTPQAASPLASWLSYLENLHSKTIDLGLERVSLVAARLGVLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYKVGVYSSPHLVRYTERVRVQGQELPESAHTASFAEIESARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSIALDHTDWLGPDRESIGREKAGIFRSEKPAIVGEPEMPSTIADVAQEKGALLQRRGVEWNYSVTDHDWAFSDAHGTLENLPLPLVPQPNAATALAALRASGLEVSENAIRDGIASAILPGRFQIVSESPRVIFDVAHNPHAAEYLTGRMKAL... | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Functions in two distinct reactions of the de novo folate biosynthetic pathway. Catalyzes the addition of a glutamate residue to dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate (7,8-dihydrofolate monoglutamate or H2Pte-Glu). Also catalyzes succes... |
P43775 | MNNMQLKATSPLAEWLSYLEKSHFKPIDLGLDRIKSVAEKLDLLHPVPYVITVGGTNGKGTTCRLLETILLNHGLRVGVYSSPHLLRYNERVRIQNQDLPDEAHTASFAFIDENKTESLTYFEFSTLSALHLFKQAKLDVVILEVGLGGRLDATNIVDSHLAVITSIDIDHTDFLGDTREAIAFEKAGIFRENCPVVIGEPNVPQTMLDQAEKLHCQVARRDVDWLFEQNAENWQWQNKKVRLENLPFCQIPLANAATVLAAVQYLPFDISEQTLRKSLQEVELVGRFQAIKTDKREKLADYLGVPVETLPTIIVDVGHN... | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Functions in two distinct reactions of the de novo folate biosynthetic pathway. Catalyzes the addition of a glutamate residue to dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate (7,8-dihydrofolate monoglutamate or H2Pte-Glu). Also catalyzes succes... |
Q05932 | MSRARSHLRAALFLAAASARGITTQVAARRGLSAWPVPQEPSMEYQDAVRMLNTLQTNAGYLEQVKRQRGDPQTQLEAMELYLARSGLQVEDLDRLNIIHVTGTKGKGSTCAFTECILRSYGLKTGFFSSPHLVQVRERIRINGQPISPELFTKYFWRLYHRLEETKDGSCVSMPPYFRFLTLMAFHVFLQEKVDLAVVEVGIGGAYDCTNIIRKPVVCGVSSLGIDHTSLLGDTVEKIAWQKGGIFKQGVPAFTVLQPEGPLAVLRDRAQQISCPLYLCPMLEALEEGGPPLTLGLEGEHQRSNAALALQLAHCWLQRQ... | Cofactor: A monovalent cation. K(+) is most effective, followed by NH4(+) and Rb(+). Na(+), Li(+) and Cs(+) are ineffective.
Function: Catalyzes conversion of folates to polyglutamate derivatives allowing concentration of folate compounds in the cell and the intracellular retention of these cofactors, which are importa... |
I6Y0R5 | MNSTNSGPPDSGSATGVVPTPDEIASLLQVEHLLDQRWPETRIDPSLTRISALMDLLGSPQRSYPSIHIAGTNGKTSVARMVDALVTALHRRTGRTTSPHLQSPVERISIDGKPISPAQYVATYREIEPLVALIDQQSQASAGKGGPAMSKFEVLTAMAFAAFADAPVDVAVVEVGMGGRWDATNVINAPVAVITPISIDHVDYLGADIAGIAGEKAGIITRAPDGSPDTVAVIGRQVPKVMEVLLAESVRADASVAREDSEFAVLRRQIAVGGQVLQLQGLGGVYSDIYLPLHGEHQAHNAVLALASVEAFFGAGAQRQ... | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Catalyzes the addition of a glutamate residue to dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate (7,8-dihydrofolate monoglutamate or H2Pte-Glu) . Also catalyzes successive additions of L-glutamate to tetrahydrofolate, leading to folylpolyglutamat... |
P36001 | MDDISGRQTLPRINRLLEHVGNPQDSLSILHIAGTNGKETVSKFLTSILQHPGQQRQRVLIGRYTTSSLLNAKEEDISINNEAISLIEYSRIEKELIEADSSLKLQCNNLELLTSVALVYFAKKNCQWCIIETGLAGKQDPGSIIAGQSRVCCAITNVGISDEAFLCKFLSQITESSTNKAIFLLDGSNDEFVRNTITKRCHDVGCPLEITDPSLRDYNVHTDTWGTLEVRLPYSEEEYQIFNLRVAIAVLDFLSKEKKVCISKDQLSQGLISVDWPRSLHRLDYCYESTSGKKIALLLDNANNAKAARNLACHLRTTYG... | Function: Conversion of folates to polyglutamate derivatives.
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + ATP + L-glutamate = (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP + H(+) + phosphate
Sequence Mass (Da): 48143
Sequence Length: 430
Pathway: Cofactor biosynthesis; tetrahydrofolylpol... |
A2RVV7 | MLMIARKALASAHTKAFRLATRDVHCFSSILVSPPLVSLDLPENWIPYSDPPPPVSFETEQKTVVIDGNVIAEEIRTKIISEVGKMKKAVGKVPGLAVVLVGEQRDSQTYVRNKIKACEETGIKSVLAELPEDCTEGQIISVLRKFNEDTSIHGILVQLPLPQHLNESKILNMVRLEKDVDGFHPLNVGNLAMRGREPLFVSCTPKGCVELLIRTGVEIAGKNAVVIGRSNIVGLPMSLLLQRHDATVSTVHAFTKDPEHITRKADIVIAAAGIPNLVRGSWLKPGAVVIDVGTTPVEDSSCEFGYRLVGDVCYEEALGV... | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da... |
Q24ZZ6 | MTQILNAKPVVQAMKENLRQEVAALQAEGKAPTLGIIRVGSRPDDVYYENNIIKNCETIGIATKTYPLDLNISMEEFTAVMTQVNDDPSVHGIMLFRPLPPQLDEEVIKHLISADKDIDCMSPLNLEKVFEGDMSGLLPCTPAAVMAILRHYEIELKGANAVVMGRSLVVGKPLSMMLLQDNATVTICHSRTRNLPEVAKNADIVIAAMGRARMIDDNYVAENSIVIDVGINDAGDGKICGDVDYDAVVDKVKAITPVPGGVGSVTTTILLNNLVRACKSQ | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da... |
Q2JCX4 | MRMLDGRSMAAEIGRYVVDEAERLAAAGVTPTLAVVLPTADPAAYSYAEIIERTAGKVGVHCVLHEPKGEPAAILDTIDTVAADPTVHGIIVQTPLPGGLTSREVGEHIPTAKDVDGMNPSSLGRLALGLPSFAPATAAAVVEILTRARIPMSGARVCVIGRGPVVGKPVSLLLLAEDATVTICHSRTKGLVSIAHEADIIVSATGHPRLVGAGFVRPGAAVIDVGTVVTETGQVGDVDAAAVSSVAGALTPVPGGVGPVTTMLLLRNTIRAARAA | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da... |
Q74GN1 | MNLLDGKKCAESLVAEIARKVAGYTESGLRTPHMTIILVGEHAPSESYVKSKIATSGLAGFESTLLRFPETIRESELLAKIKEVNEDPTTDGLIVQLPLPKHINQQHVINAIAPEKDIDGFHPANFGRMTLGQKAFRPATAYGICKLLQFYEVPVKAKHCVVIGRSNIVGKPISIMLSNDFDIGNATVTLTHIETPRELLLDETRRADIVIVAVGIPGFVTADMVKDGVVLIDVGINRLESGKIVGDVDFENVAQKCSWITPVPGGVGRMTVAALMINTLMAYQNNFNLA | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da... |
Q47IX6 | MTAQIIDGKALAEELRQGFKARVEALTAKGHKPGLVVILVGADPASEVYVRNKVNGCLAIGMHSEKITYDATIDQATVLNKIAELNADPNIHGILVQLPLPKHFDEEAVLEAISAEKDVDGFHAENVGALAQGNPRFIPCTPYGVMKMFEKGNVDLTGKEAVVIGRSNIVGKPMALLLINAGATVTVCNSRTKDLKFHTSRADILVAAVGKPKFVTGDMVKPGAVVIDVGINRLPDGKLCGDVDFASCLEVAGQITPVPGGVGPMTITMLLANTIEAAERKAGL | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da... |
Q3Z8K6 | MSAHIINGTEIAAAIREEIRSEVTALKAKHGIVPGLATVLVGDDPASHSYVDSKIKMCQNLGIYSEHHPLPQSATNEDLLTLIARLNADPKISGILVQVPLPVQISENLVLNAINPDKDVDGFHPVNVGRMCLGEPCFLPCTPHGVQELLIRSGIKIEGTHVVIVGRSNLVGKPLANILLQKAPGANATVTICHSGTKNLPLITSQADILVSAMGKPKFITADMVRQGAVVIDVGTTCIGYTPEGKRILSGDVDFEAVKEKAFAITPVPKGVGPMTIIMLMLNTLTAAKRAAGLVK | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da... |
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