ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9RW02 | MQTSSEPAASETAALLGKPLADRVMRGVRADLKAWAQLDPPFEPQLVSVLASDDEASQVYVQSKAKRAKKLGVAFRVVDLGAAATQEALEQTLRELSADPAVHGIVLELPLAAGLDADAALLHIAARKDIEGLSPANLALIAAGREPEALLPPTPRSVRFLLRHALGDDLRGLRVAVIGPGRTVGRPLLFMLNNKGATVTLCNEHTRDLAAVLAAQDAVVVAVGKAGLLRPEQVQPEHVVIDAGINVQESGDMVGDALPELPVRAQTPVPGGVGPLTSALMYQNLVRGVKLQRGEPVDD | 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... |
C0QAY0 | MAEVLKGKPVADALKAELTKNIEALKKDKGITPKLGIIRVGARPDDLFYEGGAKKTCAAVGMDCEIFEYPEDIDQASFEKAVTEVGAKKDVNGILMFSPLPKNLDERKIRTLIPVEKDVDCLTTGGAAKVFTDDATGFPPCTPTACMEMLHFYDIPIKGKKCVVVGRSLVVGKPLAMLLLREHGTVTICHSRTENLPGVCQDADILIAAVGRAKMVKADFVKKGQIVIDVGINADPDRPGKYCGDVDFETVEPVVTKITPVPAGVGSVTTSVLCKQTFMACQMQNA | 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... |
Q6ALZ5 | MSAKIISGTEIRKEILGEIKDAVTEMKDKYGTVPGLVTILVGESPASMSYVSLKIKTALSLGFYEVQESLSVETTEAELLALIEKYNNDDSIHGVLVQLPLPKHINEQNIITAIDPDKDVDAFHPVNIGRLMIGGDDVKFLPCTPAGIQEMLVRSGVETAGAEVVVVGRSNIVGKPIAMMMAQKGIGANATVTIVHTGSRDLATHCRRADILIVAAGVPNLVKPEWIKPGATVIDVGVNRVGTNSETGKAILRGDVDFEAVKEIAGKITPVPGGVGPMTIAMLMKNTLASALAHSS | 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... |
A4J3F5 | MTKILDGKKIASILREELKQDIITLKERGIEPKLAVVLVGEDPASVAYAKFLQKVSENAGVLFELHQLSKSTAEEEIICKIEDLNQIQAVHGILMMMPLPPHVNKQHIMEHISPLKDVDGLHPFNRGHLISGGICLHPATPTSCLEILKRSGITLAGKHIVVVGRGETVGKPLVFMALAENATVTVCHSRTVDLGKFTKQADIIISAVGKPGLITADMIKPGAVVVDAGIHEEAGNIIGDVDYEQVKEIAEAITPVPGGVGSLTTVLMLKNVLKGIQLQIGTQE | 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... |
Q72F91 | MQLLDGKATAATIREELRAEIAALTPRARRAPGLAVILVGEDPASQVYVRNKERACHDTGIVSEAFRLAPTTTQEELERLIADLNVRPDIDGILLQLPLPRGLDAQRCLEAIDPAKDVDGFHPQNMGRLALGLPGFRPCTPAGVMTLLERYDLSPSGRKAVVVGRSNIVGKPLALMLGAPGKYANATVTVCHSGTPDLAAECRTADFLFLAIGRPRFVTADMVREGAVVVDVGINRTETGLAGDCDFEGVSRVASAITPVPGGVGPMTIAQLLVNTVQSWKVRCGL | 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... |
A5EX57 | MSAEIINGKEIAAEIRREIKQETAQFIAATGVRPGLAVILVGNDPASEVYVRNKGIQAEEVGFLSQIYRLPAQTTQAELLAKIVALNNDPQICGILVQLPLPAHLNAEIVLNTIDPNKDVDGFHPLNIGRLWAGEPCSVPCTPLGCSLILKRYFGDSLAGKKALIIGRSNIVGKPMAALLLQQHATVTIAHSKTPDVPALCRQADIVIAAVGQPELVKGDWIKSGAVVLDVGINRIAVGDKTKLVGDVAFESAKEVAAAITPVPGGIGPMTIACLLKNTLTLAKAIQQSGK | 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... |
B8E335 | MGVILEGKPVAEKLEKEIKEKIQFYKSQGVIPTLCIVKVGKNAEAEAYAKSIEKFFSKIGINIERKNFNEEISLVDFKKIMKELEEDSAIHGVLILRPLPEELERGKAFQFLPTKKDVEGVTYENLGRLLVGEDSFHPCTPQAVLELLDFYQIPVEGKNVVVVGRSISVGKPLSLLLLNRNATITVCHSKTKNLVEFTKKAEILIVAIGKPYFVGKDMVGEGQVIIDVGTNVVDGKLVGDVNFEEVKDKVEYITPVPGGIGVITTRVLAMNLLKAVKKVEA | 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... |
A9M068 | MSAQLINGKEVSQKRLQAVAEAVAQRQQDNLHMPCLAVVLVGGDPASAVYVRNKKTACQKCGIKSLSYELPESTSQEELLALVDRLNADSEVDGILVQLPLPKHLDSQAVLERISPDKDVDGFHPYNVGRLAVKMPLMRPCTPKGVMTLLEAYGIDPKGKKAVVVGASNIVGRPQALELLLARATVTVCHSATENLADEVAGADILVVGVGIPNFVKGEWIKPGAVVIDVGINRLDDGSLCGDVEFETAKERAAMITPVPGGVGPMTIATLMENTLHAASLHDA | 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... |
Q2GCV3 | MTQLIDGFRIAAGICESIATSVAHLRKNNGLVPSLRVIIVGENPASQVYVRSKQKKAESLGIDAETIALPKDTSEVELIRLVNSLNDDTSINAILVQLPLPPHINPTRIIESIDSKKDVDCFHPENVGRLALSKDALLKPCTPAGSLYLIKSALGDNLSGMDAVVIGRSNIVGKPMAMLLLHENCTITLTHSKTRNIQEKTRQADIVISAVGIPHFVKKDFIKPGATVIDVGMNKVDGKLVGDVDFEDVLQKVKFITPVPRGVGPMTIAFLMLNTVITTCLQNKLEHQEVIGTVIQKL | 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... |
A9A4N5 | MTGTKIDGKVISQSVKDRVKKAVEELKNQGINPCLATVLVGDNPASATYVRNKHRACEEVGITTKDHKLDASTTQAQLNEIIENLNNDNSVHGILVQLPLPEQLDEFTTTSRISPLKDVDGLTPHNAGLLAMKKAALVACTPSGVMEMFDYHGIELEGKNIVLINRSNLVGKPLYHLLLDKNATVITCHSRTKNLVELCQSADIIITAVGDRNKFTLTSDMIKEGAIVIDVAISRFQEKLVGDADYEDIIQKASFATPVPGGVGPMTVAMLLKNTITAASLSSQIGK | 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... |
Q05213 | MKILRGEEIAEKKAENLHGIIERSGLEPSLKLIQIGDNEAASIYARAKIRRGKKIGIAVDLEKYDDISMKDLLKRIDDLAKDPQINGIMIENPLPKGFDYYEIVRNIPYYKDVDALSPYNQGLIALNREFLVPATPRAVIDIMDYYGYHENTVTIVNRSPVVGRPLSMMLLNRNYTVSVCHSKTKDIGSMTRSSKIVVVAVGRPGFLNREMVTPGSVVIDVGINYVNDKVVGDANFEDLSEYVEAITPVPGGVGPITATNILENVVKAAEFQKNNL | 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... |
Q9X288 | MWIDCKTIARSIEERTKERVEKLGFTPKLVSVACTDDPSALSYLKSQRKKAEKLGIAFEIMNVSPEEIVSTLKKLGSDESVNGVFVARPFPLGLDEKEILSSVPVEKDVEGVNPANLGLLLYDEEIFPPCTAEAAVRILERETNLSGKRVTVVGRSVTVGKPLALMLLKKGRDATVTVCHSRTVNLEEITKNSDIVVVAVGRAHFLKKNMVKEGAIVIDVGINYVDGKLQGDVDPSVEEIARVTPVPGGVGQVTTALLFEHVVRAAERQRK | 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... |
B9KZ23 | MAAHILSGRPVVESLHARIQQVLARRAPHQGPPTLTVLLPNDPSAQAYARAIRKQFTTLSLNYRTEEIDDTLDESRFAILLKRLAEDESVTGILALQPLPKGVSRRSLARLMPPTKDVDGVSFEQQGRLAIGSPWIAPSTPLGGLILLQHYGIEVAGRHAVVIGRSPVVGRPLALLLLARDATVTICHRRTPDLAKLTRQADLLFVAAGQPHLVKPDMVAPGAVVIDFGVSVRDGRLIGDVDPAVAEVASALTPVPGGTGPVTTAVLALNLLRLAGLLEENDLFPGAP | 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... |
Q5WE80 | MVNGINHMTFSVSNMDKAVSFYKHVFMEAPLVLGEKTAYFTIGGTWLALNLQPDIDRKEIRQSYTHIAFSIEESQLDAFYTRLLEAGADILPGRKRQVETEGKSIYFRDPDGHLLEVHTGTLAERLAHYEKTAPDMLVNIDEQNKK | Function: Metallothiol transferase which confers resistance to fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin. L-cysteine is probably the physiological thiol donor.
Sequence Mass (Da): 16647
Sequence Length: 146
Subcellular Location: Cytoplasm
EC: 2.5.1.-
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O31817 | MEIKGINHLLFSVSHLDTSIDFYQKVFGAKLLVKGRTTAYFDMNGIWLALNEEPDIPRNDIKLSYTHIAFTIEDHEFEEMSAKLKRLHVNILPGRERDERDRKSIYFTDPDGHKFEFHTGTLQDRLRYYKQEKTHMHFYDETAF | Function: Metallothiol transferase which confers resistance to fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin. L-cysteine is probably the physiological thiol donor.
Sequence Mass (Da): 17172
Sequence Length: 144
Subcellular Location: Cytoplasm
EC: 2.5.1.-
|
Q99958 | MQARYSVSDPNALGVVPYLSEQNYYRAAGSYGGMASPMGVYSGHPEQYSAGMGRSYAPYHHHQPAAPKDLVKPPYSYIALITMAIQNAPEKKITLNGIYQFIMDRFPFYRENKQGWQNSIRHNLSLNECFVKVPRDDKKPGKGSYWTLDPDSYNMFENGSFLRRRRRFKKKDVSKEKEERAHLKEPPPAASKGAPATPHLADAPKEAEKKVVIKSEAASPALPVITKVETLSPESALQGSPRSAASTPAGSPDGSLPEHHAAAPNGLPGFSVENIMTLRTSPPGGELSPGAGRAGLVVPPLALPYAAAPPAAYGQPCAQG... | Function: Transcriptional activator. Might be involved in the formation of special mesenchymal tissues.
PTM: Phosphorylation regulates FOXC2 transcriptional activity by promoting its recruitment to chromatin.
Sequence Mass (Da): 53719
Sequence Length: 501
Subcellular Location: Nucleus
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Q61850 | MQARYSVSDPNALGVVPYLSEQNYYRAAGSYGGMASPMGVYSGHPEQYGAGMGRSYAPYHHQPAAPKDLVKPPYSYIALITMAIQNAPEKKITLNGIYQFIMDRFPFYRENKQGWQNSIRHNLSLNECFVKVPRDDKKPGKGSYWTLDPDSYNMFENGSFLRRRRRFKKKDVPKDKEERAHLKEPPSTTAKGAPTGTPVADGPKEAEKKVVVKSEAASPALPVITKVETLSPEGALQASPRSASSTPAGSPDGSLPEHHAAAPNGLPGFSVETIMTLRTSPPGGDLSPAAARAGLVVPPLALPYAAAPPAAYTQPCAQGL... | Function: Transcriptional activator. Might be involved in the formation of special mesenchymal tissues.
PTM: Phosphorylation regulates FOXC2 transcriptional activity by promoting its recruitment to chromatin.
Sequence Mass (Da): 52874
Sequence Length: 494
Subcellular Location: Nucleus
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Q89WC9 | MPELPEVETVRRGLQPVMEGAKIVVAEARRPDLRFPFQPDFVARLQGQVVTGLGRRAKYLMADLASGDVLLMHLGMSGSFRVIKPDNDAAPGEFHYPRGKDTTHDHVLFRMSSGADIVFNDPRRFGYMKVIARNALEDEPLLRGLGPEPLGNEFDAAMLARSCEGKATSLKAALLDQRVVAGLGNIYVCEALHRSHLSPRRIAATLATRKGEPTDHAKRLVGAIHTVLNDAIKAGGSSLRDHRQTTGELGYFQHSFKVYDREGETCKTPACGGTIKRFTQNGRSTFWCPKCQK | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase... |
A9HI30 | MPELPEVETVMRGMRLHLDGKTIARVAVRRADLRFPFPADLVARLEGATITGFARRAKYILIRLDTGDTLLLHLGMSGRVLLSLPGDAPVPDRHEHFFFETTDGTRCGLIDPRRFGAVDLMPTAEERAHRLLARLGPEPLGNQFSQHWLQEVLARRRTSIKAALLDQTVVAGLGNIYVSEALFRAGIHPARLACTLDAAEDARLVQAIRAVLREAIAAGGSSLRDYVQPDGELGYFQHAWRVYGRAGQGCPDCPGPPACHGVERLEQAGRSSFFCPLCQPPPGKVS | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase... |
Q7VN67 | MPELPEVETCLRGIEPYLAGQTIQQIVIRTPKLRWPISAELCAMSGAKILALSRRAKYLIIHTERGDILVHLGMSGSLTLLNSSQPTKASKHDHVDLITEAGIILRYNDPRKFGAWLWAKQAENYPLITKLGPEPLSDTFTSDYLFKKSRNKTVAVKNFIMNNDIVVGVGNIYASESLFMAGVHPELAAQNLTEKQCVQLRNVIQAVLTKAIIQGGTTLKDFTQPDGKPGYFAQVLQVYGRKGEECRECGTLIQAKVIGQRNSYFCPDCQPLPK | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase... |
A1WZG2 | MPELPEVETTRRGLQVHLVGRTLQRVVVRQRQLRYPVPARVEAAVVGEEVVALERRAKYLLIRLGGGAWLLLHLGMSGSLRLVAETDAPGRHDHVDLVLNDGRAVRLTDPRRFGCLLLGDGDPQDHRLLRRLGPEPLGSAFDGAVLHRAARGRRVAVKALLMDATVVVGVGNIYANEALFRAGIRPDRAAGRIARARYDRLAGAVRAVLEAALAAGGTTLRDFTDGSGEPGYFAVNLSVYGASVCPVCGGALRQIRLAQRGTWFCPRCQR | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase... |
B0TER7 | MPELPEVETVRRSLAGRITGLTIEKVELRLPKIAFALPGTLFTDALRGRRIIELGRRGKYLLLHLDGDETLVIHLRMTGRLIHLRPEEREEPEAAHTHAVFFLDDGSLLRYTDVRQFGTLTLMTREAALRQPGKGRLGPEPLGQDFSFVDFRNALVKRKTKLKPLLLDQSFLAGLGNIYADEALARARLHPDRTADSLDDEESRRLYDCIRTVLQEGIDAKGTSFRDYVDGEGRKGEFQEKLWVYGRGGNPCRRCGGEILREKRAGRSTHFCPRCQK | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase... |
P23900 | MSNPQKALNDFLSSESVHTHDSSRKQSNKQSSDEGRSSSQPSHHHSGGTNNNNNNNNNNNNSNNNNNGNDGGNDDDYDYEMQDYRPSPQSARPTPTYVPQYSVESGTAFPIQEVIPSAYINTQDINHKDNGPPSASSNRAFRPRGQTTVSANVLNIEDFYKNADDAHTIPESHLSRRRSRSRATSNAGHSANTGATNGRTTGAQTNMESNESPRNVPIMVKPKTLYQNPQTPTVLPSTYHPINKWSSVKNTYLKEFLAEFMGTMVMIIFGSAVVCQVNVAGKIQQDNFNVALDNLNVTGSSAETIDAMKSLTSLVSSVAG... | Function: Channel protein for glycerol. Has a role in both glycerol influx and efflux. Plays a role in osmoregulation: under osmotic stress the channel is apparently closed to allow accumulation of glycerol in the cell under hyperosmotic conditions.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 738... |
P00541 | ASGQLHRPQPQEHTSTSAAAGTWRHTQASESRHRLPHCSAAPSHQDHSAMGFGPELWCPKGHSELLRLQDSELRLLELMKKWMSERAKSDREYAGMLHHMFSQLGSEEPPPALPLQEDRQSVCSTDQERSGVTALETIKNHISGIFSPRFSLPPPVPLIPEVQKPLCQQAWYHGAIPRSEVQELLKCSGDFLVRESQGKQEYVLSVLWDGQPRHFIIQAADNLYRLEGDGFPTIPLLIDHLLQSQQPITRKSGIVLTRAVLKDKWVLNHEDVLLGERIGRGNFGEVFSGRLRADNTPVAVKSCRETLPPELKAKFLQEAR... | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 60506
Sequence Length: 533
Domain: The F-BAR domain is truncated and contains only the FCH region (the coiled-coil region is missing).
EC: 2.7.10.2
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Q9NH03 | MNNQSLQRAAMISEHLAPTSELNMNQTSAPIKTAKEELADFVEIFPILTNEILKELPGMDMPPQTIAWVEKMINVNVSGGKMNRGLTVLHSLQLLVEGRQLSRSEIFLANVLGWCVEWLQAFFLVADDIMDQSITRRGQPCWYRQANPISNNGTIGSIAINDSFILESCIYILIKKYFRNEPYYADILDIFHETSYQTELGQLLDLTTQPNRGDFSLFTLNTYRRIVKYKTAYYSFYLPVALAMLMAGITSTPAFSTAKDILLPMGEFFQVQDDFLDCYGSPAVIGKIGRDIEENKCSWMICQAILNGTPEQINLLKKHY... | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a sterol precursor. Involved in the inhibition of cell growth.
Catalytic Activity: dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diph... |
Q4JHN6 | MSDLKTRFLEVYSVLKSELLNDPAFEFTDDSRQWVERMLDYNVPGGKLNRGLSVIDSYKLLKEGKELSDDEIFLSSALGWCIEWLQAYFLVLDDIMDSSHTRRGQPCWFRLPKVGMIAVNDGILLRNHIPRILKKHFRQKPYYVDLLDLFNEVEFQTASGQMIDLITTLVGEKDLSKYSLPIHRRIVQYKTAYYSFYLPVACALLMSGEDLEKHTNVKDILIEMGTYFQVQDDYLDCFGAPEVIGKIGTDIEDFKCSWLVVKALELSNEEQKKFLHENYGKDDPASVAKVKELYNTLKLQDVFAEYESKSYDKLIKFIEA... | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (By similarity). Component of the triterpe... |
P42512 | MKTETKVIKGRQGIARNRHTPLCLGLLLALSPLAAAVADARKDGETELPDMVISGESTSATQPPGVTTLGKVPLKPRELPQSASVIDHERLEQQNLFSLDEAMQQATGVTVQPFQLLTTAYYVRGFKVDSFELDGVPALLGNTASSPQDMAIYERVEILRGSNGLLHGTGNPAATVNLVRKRPQREFAASTTLSAGRWDRYRAEVDVGGPLSASGNVRGRAVAAYEDRDYFYDVADQGTRLLYGVTEFDLSPDTLLTVGAQYQHIDSITNMAGVPMAKDGSNLGLSRDTYLDVDWDRFKWDTYRAFGSLEQQLGGGWKGK... | Function: High-affinity outer membrane receptor required for the transport of Fe(3+)-pyochelin.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 79992
Sequence Length: 720
Subcellular Location: Cell outer membrane
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P42513 | MPRQSGFGWAWRVPLALAGSLAAATASGYLLTRGLPLDDPLERLYAGLFGALGVGLLLLVGGLLARGPGNFAWRLGGSLLVLGLALWLLAGRG | Function: May play some role in transport of Fe(3+)-pyochelin.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 9569
Sequence Length: 93
Subcellular Location: Cell membrane
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Q81L65 | MKKILSIFIVVFLFAVGCGQQKEEKKETKADNKNQAITIKHAEGETKLDKPAKKVVVLEWVYSEDLLALGVQPVGMADIKNYNKWVNTKTKPSKDVVDVGTRQQPNLEEISRLKPDLIITASFRGKAIKNELEQIAPTVMFDPSTSNNDHFAEMTETFKQIAKAVGKEEEGKKVLADMDKAFADAKAKIEKADLKDKNIAMAQAFTAKNVPTFRILTDNSLALQVTKKLGLTNTFEAGKSEPDGFKQTTVESLQSVQDSNFIYIVADEDNIFDTQLKGNPAWEELKFKKENKMYKLKGDTWIFGGPESATSLATQVADVM... | Function: Part of an ABC transporter complex involved in ferric-petrobactin uptake.
Location Topology: Lipid-anchor
Sequence Mass (Da): 36074
Sequence Length: 324
Subcellular Location: Cell membrane
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Q81L64 | MNNLQHTLRASLVFGGGGALLLLLFFIHIGQGQANISYSMIIDALISPNQSLEHQTLIMLRLPRAVIAILAGGALAASGVILQTLTKNPLAESSTMGIHSGAYFFLVAATIFLPKGLQINSLLFTFIGGAITALFVYRISGEKKGTPLRMALAGMVVTLMLSAFTGTMQLFYENETAGLFLWGAGSLIQNNWDGVQFSFPFIIISFLVLLGISRKLNILLLGDDVAVSLGEKTAVTRLIAFIAAIFLTAVIVTVVGPIGFVGLVAPHLMRLIGYRQHFTLLLSSFLWGAVLLLGADVAGRLIDPTGAELPVGAVTAMIGS... | Function: Part of an ABC transporter complex involved in ferric-petrobactin uptake. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 72025
Sequence Length: 678
Subcellular Location: Cell membrane
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Q81LM1 | MISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLMARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQMHDHQLDLTVKELIEFGRGPHKSWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGVPEEVLCHEMFQHIFGIEVDIFQGSEKPFFTPKRISKKGGAKCEQKNVLPLS | Function: Part of an ABC transporter complex involved in ferric-petrobactin uptake. Probably responsible for energy coupling to the transport system.
Catalytic Activity: a Fe(III)-siderophore(out) + ATP + H2O = a Fe(III)-siderophore(in) + ADP + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Ma... |
Q81V82 | MQKALETKRLTLSYGETIIIDELNLEIPKGEITIFIGSNGCGKSTLLRSLARLLKPTTGDILLDNQAIQSMQTKQIARQMAILPQGPQAPEGLTVLQLVKQGRYPYQTWLKQWSEKDEEMVQNALAATGMTEFAERDVHALSGGQRQRAWIAMTLAQDTDIILLDEPTTYLDMTHQIEVLDLLFELNETEQRTIVMVLHDLNLACRYADNIVAIQDKQIYAQGKPEEVVDEKLVRDVFRMECQISTDPLFGTPLCIPHGKGRRVRKEVAHAMR | Function: Part of an ABC transporter complex involved in ferric-petrobactin uptake. Probably responsible for energy coupling to the transport system.
Catalytic Activity: a Fe(III)-siderophore(out) + ATP + H2O = a Fe(III)-siderophore(in) + ADP + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Ma... |
P48632 | MPAPHGLSPLSKAFLMRRAFQRRILPHSLAMALSLPLAGYVQAQEVEFDIPPQALGSALQEFGRQADIQVLYRPEEVRNKRSSAIKGKLEPNQAITELLRGTGASVDFQGNAITISVAEAADSSVDLGATMITSNQLGTITEDSGSYTPGTIATATRLVLTPRETPQSITVVTRQNMDDFGLNNIDDVMRHTPGITVSAYDTDRNNYYARGFSINNFQYDGIPSTARNVGYSAGNTLSDMAIYDRVEVLKGATGLLTGAGSLGATINLIRKKPTHEFKGHVELGAGSWDNYRSELDVSGPLTESGNVRGRAVAAYQDKHS... | Function: Receptor for the siderophore ferripyoverdine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 91167
Sequence Length: 815
Subcellular Location: Cell outer membrane
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A0A1L7U2E9 | MSLPKAQILVVVTVGGSTNSAPILEICSILAARGHTIDFATLSGRQKLVDNYPFVKKVHIVGPAISAEEDEKHYILFSRWNWNTARGKRDIVKGKMAFDAFWPFTYRGLKEVITTTKPDFIFSDFHVEAALDVCNEFRLPHAVMWPQMPWLMMPQKYIPGQPGMQQRCLTSEHASIYDRLFEMTFLLRSAPFFLHWIFWTKAMRRKEGVAPRPRHSKPDYLVFMNNFYGMETPRDTPPLVHPVGPILADSYPALDGDIKSFVETHQKIALVAFGTHVILDDGKIFKIIDGLADAISSGVIDGVVWALSARSRGQLDTSIR... | Function: UDP-glycosyltransferase; part of the gene cluster that mediates the biosynthesis of the gamma-pyrones fusapyrone (FPY) and deoxyfusapyrone (dFPY) (Ref.2). FPY is an undecaketide and thus likely synthesized by the polyketide synthase FPY1 from acetyl-CoA functioning as starter unit and the addition of 10 malon... |
A0A1L7TZY0 | MRILCLHGMGTNSKVLEMQTSALRHQLSHSQSHKYEYVDGGEPMPPAPGIEAFIGQDESLAYYHPHSAKSILTAIDDLWEYIAEEGPFDGVLGFSQGASLAAMIIARAHHSDPPPFQFAIFFCAGLPYCEKSLSAGEVKFLRAEATQGPVIHVPTAHIFGKKDPDVSYSKAMTELCHPWGRVLLDHGAGHEIPRVPVETVDDMARAVEKVVTKAVIGQ | Function: Esterase; part of the gene cluster that mediates the biosynthesis of the gamma-pyrones fusapyrone (FPY) and deoxyfusapyrone (dFPY) (Ref.2). FPY is an undecaketide and thus likely synthesized by the polyketide synthase FPY1 from acetyl-CoA functioning as starter unit and the addition of 10 malonyl-CoA extender... |
A0A1L7TV57 | MPNLEKEFHNGVNGLNGNTKIENDGCVNPHSLGIIGGGWYGCHIAATLLALGFRVKLFEQHERLLHEASGNNQFRLHMGFHYARHSGTRLQSRDGFLRFVEHYPELSRIVPYNIYAVPTQDSLLDYNTYKAIMASSGVAFTEGAPDGVHITNVDGIMCVPERVLLLTKARAYFEAALKGALELGRKVSSIQEADDGVLIDGEGFDFVVDATWGHYMDLDLQVIYEATLLLYYEGPPEFPAVTLVDGPLASVYPTEVPGVFTLSSVPHTPLGQFKTAAEARAARDGVSPATISAKRALMEEQIMHYLPTFLETFRYIGPQL... | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the gamma-pyrones fusapyrone (FPY) and deoxyfusapyrone (dFPY) (Ref.2). FPY is an undecaketide and thus likely synthesized by the polyketide synthase FPY1 from acetyl-CoA functioning as starter unit and the addition of 10 m... |
A0A1L7TV54 | MSETTGLPLKHLQGSPPGTPVNTNNESNEASPDDGCRLPDTVTEAEASSDNHGSVLGDNNRNVEVAVGASDNATKQKVYHTGWRLHALTSALCLSLLLSTLETTIVSTALVSIVDALHGFNMAGWIVTSYLVTYTGFLIIYSKLSDIFGCKLMLLLAITIFTVFSMACGASDSMVPLIVFRAFQGMGGSGIYSLSTIMVPLMVPPEKYATYISIMSSTFILSSVLGPILGGAITDHTTWRWVFYFNGPGGALAAVLLAFSVPFNFPYGESDRFFHSLASKQMWKRVDFVGMTVSLAASILIIFALEQGGVAYPWGSGAIV... | Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of the gamma-pyrones fusapyrone (FPY) and deoxyfusapyrone (dFPY).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64433
Sequence Length: 597
Pathway: Secondary metabolite biosynthesis.
Subcellular Location: Membra... |
A0A1L7U5T4 | MVGIALLGAGIFAREQHLPAIESVGHLNLKAVYSRSEEAAISLAKQARDRVDIYFDSPPTSGRSLDDLLARSDIAAVAACATILVQPLLIRKALRAGKHVLSEKPIAQDTATAMGLVQWYSSQSSPPIWAVAENFRFNESLRYAEMRTQEIGGELASFRLTYYGLIRKENKYFKTEWRKTPEFQGGFLLDSGIHFIASLRLLLRAVGQEPKEVMALSSLLKEHLHPVDTIHAVVSTIDSRHGTVCISFGVEHISTLEIEIISTRGVIVWTPVSVTSIIKSDSGESMNEKKEFIYNNGVKAEFEAFCQAILQNSPDPRQSP... | Function: Dehydrogenase; part of the gene cluster that mediates the biosynthesis of the gamma-pyrones fusapyrone (FPY) and deoxyfusapyrone (dFPY) (Ref.2). FPY is an undecaketide and thus likely synthesized by the polyketide synthase FPY1 from acetyl-CoA functioning as starter unit and the addition of 10 malonyl-CoA ext... |
A0A1L7TV75 | MAIIPWKAIDESLSLRWKIIVTLLAIYTLRIIGTRITTTRARRKFREQHGCAPVTCQLPLKDPFFGIDFILKLMRVFKEKRLLETFANDFYKTVGITFLVERGSQQTIFTIDPENIKTVLALKFKDYGLAFRAPLFNPVTGGGMFVSDGEEWAHSRALMRPTFARDQVADLALTNRHVTDLVSKIPINTTFNLQELLFDFTMDTGTEFLFGESTDTLCNPTKASQEFTKAFDFTLKDVAYQARLGPLRRFQGSRSKALEVYQVCRSYVERYVDQAMALRTSTLTGEVTRENEPQNRHDSLLRQLARSGVSKEKIRAELLS... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the gamma-pyrones fusapyrone (FPY) and deoxyfusapyrone (dFPY) (Ref.2). FPY is an undecaketide and thus likely synthesized by the polyketide synthase FPY1 from acetyl-CoA functioning as starter unit and the addition of 10... |
P80489 | MTKVVEISPTTRLEGHSKLTLKVDDQGIVERGDWLSITPVRGIEKLAIGKTMEQVPKIASRVCGICPIAHTLASTEAMEASIGCEIPTDAKLLRTILHAANRIHSIALHNILILPDFYIPGTEKKFNLFANEQPARSVMARIVRIREIAQTIGAIAGGEAIHPSNPRIGGMYYNVSPRAKQKMADLAKEGLVLVHEQMEFMFDVIRNMQNREFVEVAGKQIPLPKKLGYHNQGVMATASMYGSSSLDDNPTWDFTRWKETRPWDWYMGEVTIDLEDPSYPIGGTTKIGTKANPQMEACTGVPTYDGQPVEVGPRARLATF... | Function: Reduces the physiological low-potential two-electron acceptor coenzyme F420, and the artificial one-electron acceptor methylviologen.
Catalytic Activity: H(+) + H2 + oxidized coenzyme F420-(gamma-L-Glu)(n) = reduced coenzyme F420-(gamma-L-Glu)(n)
Location Topology: Peripheral membrane protein
Sequence Mass (D... |
Q60338 | MEVNFVTNRIEIAPTTRHEGHAKLILEVDEEGIVNKAYYLNTTPVRGFETMLKGKPAEFAPIAVMRICGICQTTHGIASCEAIENAIDCEVPDDGLLLRELVGIGNRLHSHPLHHLLTIDDFLKPDETDLKIELIKLIQRMRKVGQLVVDIVGGEGIHPPNIVIGGMRTNITERAKSRLYYALRQYEKDAYELYEKYTELIERYLEEIGIPDLGAHEYPYIATHTTYGDRYAINWDDVTEIPAQRYYDDEEAKQTTTIQIPLYAGVPAEGGPRARMVKFGNFREGGSAMDINIARAQENLGAVYRALEILDELDLNGKTR... | Cofactor: There are 12-13 Fe atoms/(alpha(1)beta(1)gamma(1)) unit of the FRH.
Function: Reduces the physiological low-potential two-electron acceptor coenzyme F420, and the artificial one-electron acceptor methylviologen.
Catalytic Activity: H(+) + H2 + oxidized coenzyme F420-(gamma-L-Glu)(n) = reduced coenzyme F420-(g... |
P19496 | MSERIVISPTSRQEGHAELVMEVDDEGIVTKGRYFSITPVRGLEKIVTGKAPETAPVIVQRICGVCPIPHTLASVEAIDDSLDIEVPKAGRLLRELTLAAHHVNSHAIHHFLIAPDFVPENLMADAINSVSEIRKNAQYVVDMVAGEGIHPSDVRIGGMADNITELARKRLYARLKQLKPKVDEHVELMIGLIEDKGLPKGLGVHNQPTLASHQIYGDRTKFDLDRFTEVMPESWYDDPEIAKRACSTIPLYDGRNVEVGPRARMVEFQGFKERGVVAQHVARALEMKTALARAIEILDELDTSAPVRADFDERGTGKLG... | Cofactor: There are 12-13 Fe atoms/(alpha(1)beta(1)gamma(1)) unit of the FRH.
Function: Reduces the physiological low-potential two-electron acceptor coenzyme F420, and the artificial one-electron acceptor methylviologen.
Catalytic Activity: H(+) + H2 + oxidized coenzyme F420-(gamma-L-Glu)(n) = reduced coenzyme F420-(g... |
Q00390 | MGKTVEINPTTRHEGHTKLVLKVDDDGIVEKGNYLSVTPVRGFEKFLVGKPAEFAPIAVSRFCGICPIAHATSAVEAIEDACGIVPPKDGLLLRELTGLGNKMHSHPLHEFLIAPDFIPEKDRVEYITRIQQMRKTGQYIVDTIGGEAIHAPNIKVGGMLKSITPSAVSKIYYKCKEFEKLAKEQVEYLIPIFENRTLVDGTEIPEKLGYHDFGYLATDSTYGNRENIEQKKVHEYTPYDVYEKEVAVQACQLFQEYNGRLMEVGPRARFAKFHDFKEKGAMAIHIARAYENVIHVKRAMEIIEELNVDGLTRAKDPILG... | Function: Reduces the physiological low-potential two-electron acceptor coenzyme F420, and the artificial one-electron acceptor methylviologen.
Catalytic Activity: H(+) + H2 + oxidized coenzyme F420-(gamma-L-Glu)(n) = reduced coenzyme F420-(gamma-L-Glu)(n)
Sequence Mass (Da): 44612
Sequence Length: 398
EC: 1.12.98.1
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P19499 | MVLGTYKEIVSARSTDREIQKLAQDGGIVTGLLAYALDEGIIEGAVVAGPGKEFWKPEPMVAMTSDELKAAAGTKYTFSPNVLMLKKAVRQYGIEKLGTVAIPCQTMGIRKAQTYPFGVRFVADKIKLLVGIYCMENFPYTSLQTFICEKLGLNMELVEKMDIGKGKFWVYTQDDVYTLPLKETHGYEQAGCKICKDYVAELADVSTGSVGSPDGWSTVITRTDSGDSILKQAVEAGIFETKPIEEVKPGLGLLEKLSAQKKEKAEKNIAARKEMGLPTPY | Cofactor: There are 12-13 Fe atoms per alpha/beta/gamma unit of the FRH.
Function: Reduces the physiological low-potential two-electron acceptor coenzyme F420, and the artificial one-electron acceptor methylviologen.
Catalytic Activity: H(+) + H2 + oxidized coenzyme F420-(gamma-L-Glu)(n) = reduced coenzyme F420-(gamma-... |
P80491 | MTNKIKIGHVHMSGCTGCLVSLADNNLGLIKILDDYADLVYCLTLADVRHIPEMDVALVEGSVCLQDHESVEDIKETRKKSKIVVALGSCACYGNITRFSRGGQHNQPQHESYLPIGDLIDVDVYIPGCPPSPELIRNVAVMAYLLLEGNEEQKELAGKYLKPLMDLAKRGTSGCFCDLMYDVINQGLCMGCGTCAASCPVHAITLEFGKPQGERDLCIKCGSCYGACPRSFFNLDVIPEFENINEIIANALKEGESDD | Function: Reduces the physiological low-potential two-electron acceptor coenzyme F420, and the artificial one-electron acceptor methylviologen.
Catalytic Activity: H(+) + H2 + oxidized coenzyme F420-(gamma-L-Glu)(n) = reduced coenzyme F420-(gamma-L-Glu)(n)
Sequence Mass (Da): 28241
Sequence Length: 259
EC: 1.12.98.1
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P19498 | MAEENAKPRIGYIHLSGCTGDAMSLTENYDILAELLTNMVDIVYGQTLVDLWEMPEMDLALVEGSVCLQDEHSLHELKELREKAKLVCAFGSCAATGCFTRYSRGGQQAQPSHESFVPIADLIDVDLAIPGCPPSPEIIAKAVVALLNNDMEYLQPMLDLAGYTEACGCDLQTKVVNQGLCTGCGTCAMACQTRALDMTNGRPELNSDRCIKCGICYVQCPRSWWPEEQIKKELGL | Cofactor: There are 12-13 Fe atoms per alpha/beta/gamma unit of the FRH.
Function: Reduces the physiological low-potential two-electron acceptor coenzyme F420, and the artificial one-electron acceptor methylviologen.
Catalytic Activity: H(+) + H2 + oxidized coenzyme F420-(gamma-L-Glu)(n) = reduced coenzyme F420-(gamma-... |
Q00393 | MVKIAHIHMSGCTGCLISLTDTYEKLLDILGSVELVYALTLTGEKTEITETDDKILIERDIPGGIDIALVEGSVCLDDHHSMDDILTTRKNSKKSLVALGACAASGGVTRFRRVGQMSQPSHASFVPIGDVIKVDLALPGCPPSTESIVKLLTAALEGDMEYLEPFAEIAKYGKDACGCDVIKEVINKSLCMGCGTCAAACQVNAIDMVEAKPNINSEFCIKCGICSAQCPRVRFPEIIRKLE | Function: Reduces the physiological low-potential two-electron acceptor coenzyme F420, and the artificial one-electron acceptor methylviologen.
Catalytic Activity: H(+) + H2 + oxidized coenzyme F420-(gamma-L-Glu)(n) = reduced coenzyme F420-(gamma-L-Glu)(n)
Sequence Mass (Da): 26040
Sequence Length: 243
EC: 1.12.98.1
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Q39101 | MASNALSSFTAANPALSPKPLLPHGSASPSVSLGFSRKVGGGRAVVVAAATVDTNNMPMTGVVFQPFEEVKKADLAIPITSHASLARQRFADASEAVINEQINVEYNVSYVYHSMYAYFDRDNVAMKGLAKFFKESSEEERGHAEKFMEYQNQRGGRVKLHPIVSPISEFEHAEKGDALYAMELALSLEKLTNEKLLNVHKVASENNDPQLADFVESEFLGEQIEAIKKISDYITQLRMIGKGHGVWHFDQMLLN | Function: Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation (By similarity).
Catalytic Activity: 4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O
Sequence Mass (Da): 2817... |
Q96540 | MASKALSSFTAKPAVSLLPHGVSSSASPSVMSLSFSRHTGGRGVVAASSTVDTNNMPMTGVVFQPFEEVKKADLAIPITSNASLARQRYADSSEAAINEQINVEYNVSYVYHSMYAYFDRDNVALKGLAKFFKESSDEEREHAEKFMEYQNQRGGRVTLHPIVSPISDFEHAEKGDALYAMELALSLEKLTNEKLLNLHRVASENNDPQLADFVESEFLGEQIEAIKKISDFITQLRMVGKGHGVWHFDQMLLN | Function: Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation (By similarity).
Catalytic Activity: 4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O
Sequence Mass (Da): 2816... |
P36088 | MGSSTGFHHADHVNYSSNLNKEEILEQLLLSYEGLSDGQVNWVCNLSNASSLIWHAYKSLAVDINWAGFYVTQASEENTLILGPFQGKVACQMIQFGKGVCGTAASTKETQIVPDVNKYPGHIACDGETKSEIVVPIISNDGKTLGVIDIDCLDYEGFDHVDKEFLEKLAKLINKSCVFK | Function: Catalyzes the reversible oxidation-reduction of the R-enantiomer of free methionine sulfoxide to methionine. Does not act on S-enantiomer of free methionine sulfoxide or R-enantiomer of dabsylated methionine sulfoxide. Involved in protection against oxidative stress.
Catalytic Activity: [thioredoxin]-disulfid... |
Q9LMM2 | MGVGEMNKEVIDKVIKFLMMVILMGTIVIWIMMPTSTYKEIWLTSMRAKLGKSIYYGRPGVNLLVYMFPMILLAFLGCIYLHLKKSTTVNQFNSGVEKKRAKFGALRRPMLVNGPLGIVTVTEVMFLTMFMALLLWSLANYMYRTFVNVTSESAATDGNNLWQARLDLIAVRIGIVGNICLAFLFYPVARGSSLLAAVGLTSESSIKYHIWLGHLVMIIFTSHGLCYFIYWISKNQLVSKMLEWDRTAVSNLAGEIALVAGLMMWVTTYPKIRRRLFEVFFYSHYLYIVFMLFFVFHVGISHALIPLPGFYIFLVDRFLR... | Function: Ferric chelate reductase involved in iron reduction in roots (By similarity). May participate in the transport of electrons to a Fe(3+) ion via FAD and heme intermediates.
Catalytic Activity: 2 a Fe(II)-siderophore + H(+) + NAD(+) = 2 a Fe(III)-siderophore + NADH
Location Topology: Multi-pass membrane protein... |
P92949 | MEIEKSNNGGSNPSAGEEFKDMIKGVTKFLMMVIFLGTIMLWIMMPTLTYRTKWLPHLRIKFGTSTYFGATGTTLFMYMFPMMVVACLGCVYLHFKNRKSPHHIDRETKGGVWSKLRKPMLVKGPLGIVSVTEITFLAMFVALLLWCFITYLRNSFATITPKSAAAHDESLWQAKLESAALRLGLIGNICLAFLFLPVARGSSLLPAMGLTSESSIKYHIWLGHMVMALFTVHGLCYIIYWASMHEISQMIMWDTKGVSNLAGEIALAAGLVMWATTYPKIRRRFFEVFFYTHYLYIVFMLFFVLHVGISFSFIALPGFY... | Function: Flavocytochrome that transfers electrons across the plasma membrane to reduce ferric iron chelates to form soluble ferrous iron in the rhizosphere. May be involved in the delivery of iron to developing pollen grains. Acts also as a copper-chelate reductase. Involved in glycine betaine-mediated chilling tolera... |
F4I4K7 | MAARGRLVVARGNRSFSSIIRKYSLKRETNKKVIKNVIKLLTMVILMGTVVIWIMMPTSTYKKIWLKSMRAKLGKSIYFGKPGVNLLVYMFPMILLASLGSIYLHLKKQTRVNQFNSRMDRKKIDKFGALKRPMLVKAGLGIVTVTEVMFLMMFMALLLWSLANYFYHTFVTITPQSLPTDGDNLWQARLDSIAVRLGLTGNICLGFLFYPVARGSSLLAAVGLTSESSTKYHIWLGNLVMTLFTSHGLCYCIYWISTNQVSQMLEWDRTGISHLAGEIALVAGLLMWATTFPAIRRRFFEVFFYTHYLYMVFMLFFVFH... | Function: Ferric chelate reductase involved in iron reduction in roots. May participate in the transport of electrons to a Fe(3+) ion via FAD and heme intermediates.
Catalytic Activity: 2 a Fe(II)-siderophore + H(+) + NAD(+) = 2 a Fe(III)-siderophore + NADH
Location Topology: Multi-pass membrane protein
Sequence Mass (... |
Q9FLW2 | MGNMRSLVKMLMVVLFLGWIFVWIMISTNRFQNIWTPKLAKYLKTTYFGPQGMNLVLLTVPMMFIAVLSCVYLHTQKQPSQTQSLYKCREWKVKGRMGRVMMVMNPLGIVTATELTFSLLFLALLVWALSNYLYLSYHVHLHNHDNANDMCRWQAKFRAFGLRIGYVGHYCWAFLFFPVTRASTILPLVGLTSESSIKYHIWLGHVSNFCFLVHTVVFLIYWAMVNKLMETFAWNATYVPNLAGTIAMVIGIAIWVTSLPSFRRKKFEIFFYTHHLYGLYIVFYAIHVGDSWFCMILPNIFLFFIDRYLRFLQSTKRSRL... | Function: Ferric chelate reductase probably involved in iron reduction in shoots. May participate in the transport of electrons to a Fe(3+) ion via FAD and heme intermediates. May act in iron metabolism in reproductive organs . May function as root surface cupric chelate reductase and participate in the reduction of Cu... |
Q3KTM0 | MDDHETPLLSKDLSSSSSSSSSSSSVVVSSLKWILKVVMSVIFVTWVVFLMMYPGSLGDQILTNWRAISSNTLFGLTGSMFLIFSGPILVIAILASLYLIISGEETVFTKKKITKFPRFRLWTFPVLVDGPFGVVSAAEFLGIMVFSVFFLWAIYAYTLRNLNVLDYFHVLPNNRSIFLLELTGLRFGMIGLLCMVFLFLPISRGSILLRLIDIPFEHATRYHVWLGHITMTFFSLHGLCYVVGWTIQGQLLELLFEWKATGIAVLPGVISLVAGLLMWVTSLHTVRKNYFELFFYTHQLYIVFVVFLALHVGDYLFSIV... | Function: Ferric chelate reductase involved in iron mobilization from the cytosol into the chloroplast. May participate in the transport of electrons to a Fe(3+) ion via FAD and heme intermediates. Might be involved iron homeostasis in trichomes.
Catalytic Activity: 2 a Fe(II)-siderophore + H(+) + NAD(+) = 2 a Fe(III)-... |
Q8VY13 | MAKVLTLLVLRLLMNLLLIGWISLWIIKPTTIWIQSWRQAEDTARHTFFGYYGLNFAVFSFPPIALSIVGLIYLSLLPQHHHPTRGGRGAAITVSRPAIINSFIGIVSCFEILALLLFLLFLAWNFYARVSNDFKKLMPVKTMNLNLWQLKYYRVATRFGLLAEACLSLLLFPVLRGLSMFRLLNIEFAASVKYHVWFGTGLIFFSLVHGGSTLFIWTITHHIEEEIWKWQRTGRVYVAGLISLVTGLLMWITSLPQIRRKNFEVFYYTHHLYIVFLVAFLFHAGDRHFYWVLPGMFLFGLDKILRIVQSRSESCILSAN... | Function: Ferric chelate reductase probably involved in iron reduction in leaf veins for transport. May participate in the transport of electrons to a Fe(3+) ion via FAD and heme intermediates.
Catalytic Activity: 2 a Fe(II)-siderophore + H(+) + NAD(+) = 2 a Fe(III)-siderophore + NADH
Location Topology: Multi-pass memb... |
Q04800 | MAINSSDKWTVIAICLILGILLAFILMFWLERFRVIIKSNAHKHDPSDKRQIWLEKYYLFVRQIYTYLVTHKVILTLIAVPVVFAISIPFIGMQTPASSHGKQTTQVSTGNWSKNAVAARLGFLACGLYVTSYFFSIKNNPFALLLISSHEKMNYVHRRLSQYAIMIGAIHGFAYIGLAAQGKRALLTARVTIIGYVILGLMVIMIVSSLPFFRRRFYEWFFVLHHMCSIGFLITIWLHHRRCVVYMKVCVAVYVFDRGCRMLRSFLNRSKFDVVLVEDDLIYMKGPRPKKSFFGLPWGAGNHMYINIPSLSYWQIHPFT... | Function: Metalloreductase responsible for reducing extracellular iron and copper prior to import (By similarity). Catalyzes the reductive uptake of Fe(3+)-salts and Fe(3+) bound to catecholate or hydroxamate siderophores (By similarity). Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can ... |
O94727 | MILARDDKWTLGSIALIFVLLIGFALLFLLERFRVKEKSRTFKDCVNVYQCPSKGERVYLALRHWFIFLATHKAQMTLILSPLVMLVTIPFTGKETKNSIASYDWNLTGVAARLGYLSCGLFFVSYFFSLKNNPFCLMLFSSHEKMNYLHRWLSVYAVLISVLHGILFMIFSAQSYKPLLYDKISIYGYFITVVLFLMTVASLPSVRRKFFEWFFVLHHTCSVLIIFLIWLHHPRTIVYMKACIIIYAFDRGCRLFRSIWNRSNFRIYLLNEDMIYMVGRKPKRSFFALPWAAGSHVYINIPSLSYWQVHPFTLASAPFD... | Function: Metalloreductase responsible for reducing extracellular iron and copper prior to import (By similarity). Catalyzes the reductive uptake of Fe(3+)-salts and Fe(3+) bound to catecholate or hydroxamate siderophores (By similarity). Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can ... |
I1S165 | MTIQSTANHQDGYLPAILCLHGAGTNATIFNLQARTIVRCLKHKFRFIFVNAPFESLPGPGVIPTFAEIRPYLRWHCDENAIQEFDVSPELVDNERRLVRSMISDKIEQEATGPSLGIVGVMAFSQGTRVATGLCLDPEFGSSIQFAIIIAGTFPALSLENPVSDSETTNLFSGINGNKHEQLQIPSVHVQGTMDPWGPESARLLKECWSADLAMVVKFHGAHQVPTSKKDAQAVAQAVLSCWDSAQT | Function: Thioesterase; part of the gene cluster that mediates the biosynthesis of fusarielins F, G and H, decaketide compounds with 5 methylations and a decaline core that act as mycoestrogens as they stimulate growth of MCF-7 breast cancer cells . The initial compound in the pathway is produced by the reducing polyke... |
A0A0E0RXA9 | MSVTRLSEPLQNILLQDLRNFYDRASRIATLSVSAIAAIKSAWTRGSPFAAATALYPTNEEGKYVIQAEGIRMEFTNYGGAVTNLWLNNSRGEEVDIVLGLDHARDYEDYPKNPYLNGAIGRYAGFMRGGRFDMDGESYQVATNAHNGSSTFNGGDRGWGRSILDIGSHTENSITFVLFDRSWNGFPGTAASCLTHTVTPYEWRVAFGVTPTKKPGPINMSQQAFFNLDGFKKKNLTGSVPVSDKTVRDHKLHLPLSGLRFETDALGLSTGDILGNPRGSEYDFWSASRRIGDVLEKPYMGICDRCQKRQYHNHNPSGAY... | Function: Epimerase; part of the gene cluster that mediates the biosynthesis of fusarielins F, G and H, decaketide compounds with 5 methylations and a decaline core that act as mycoestrogens as they stimulate growth of MCF-7 breast cancer cells . The initial compound in the pathway is produced by the reducing polyketid... |
I1S163 | MSVIGLWLVTVTATLSLFVWQLIFLLSIPKSIVVCLIAESLFFVAWFFYWTVIYPRYLTPFRHLPTPASRSILTGNQNGLFTENSWDVARRVSQTVPNSGLIRYYVALSNERILVTNTRALSDVLTNHSHDFGKSNLAKFALKRLTGNGLGFLEGNEHKVHRKNLMPAFTRKHVKELTPIFWDKAMEMVKGMEAEVRCGKDTSTQGTGIVEIHDWATRATLDIIGTAGFGYDFGTLHNPSNEIGQQYKKMFLEPSTAFNWLELLGNYIDFRFLMTLPVKKNRDLTAGSNFMREIAKKVIRERRHELFQRMTSQAGNMKNT... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fusarielins F, G and H, decaketide compounds with 5 methylations and a decaline core that act as mycoestrogens as they stimulate growth of MCF-7 breast cancer cells . The initial compound in the pathway is produced by th... |
A0A0E0RXA7 | MTNLPSHHTAIVGSEDGSLKVAEQVPLPRLENDMILVRNTAVALNPIDGKMVGNLASVGAVAGMDYVGTVVGIGPKVKTASEIQLGDRVCGAVQGMHSLTPSVGAFAQFVGATDIVTLKVPPSMTVEDAATLGSGVGTIGLALFRSLDVPGYPEAPATERIPVLVYGGSTATGTLAIQLLKLSGLIPITTCSPHNFDLVKSFGAEAVFDYRRPETPDEIRKFTRNSLKYVLDCISEPETMQFCYKCIGRTGGKYTALEPFPQFLHTRPTIQPDWVLGPTLLGKPIGWGPPFERVGDPDVREFAIKWFATAQRLLDQGKLQ... | Function: Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of fusarielins F, G and H, decaketide compounds with 5 methylations and a decaline core that act as mycoestrogens as they stimulate growth of MCF-7 breast cancer cells . The initial compound in the pathway is produced by the reduci... |
Q556J4 | MVSNKNLLPIIYIFFIILYFGDVAKSQYFPLDKGATCQKYRGDSPGIQLCDGFLSNPNSIYINSTSSQEAIQAQGNLVRQYINFYKSFESCKNPRTFALLCAFLFPECEKYTDPVSKVTYAYPILPCYNNCLNMTTSCQISTSRLSCATKYTFENISYSVFPKNTTTYQIDSLSYTNTCENTDLIANSQNTSIQQCFEPLVYHVSTDEIHDKSIGYIFPSTNTTCVVGCPAPLYYANQWRNIYRLSDVLSILSCILTLFLVITLGIINPKVSRFDKINVMLLSSIFLQAFSGALMTFNGTENTLCPEDGRFASYIDRMCV... | Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68945
Sequence Length: 607
Domain: Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl (Disheveled) family members and is involved in the activation of the Wnt/beta-catenin signaling pathway.
Subcellular Location: Membrane
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A4J0S6 | MKKVPSDLEIAQAHEMIPIAEIAKNIGLGEDDIDLYGKYKAKISLDVLRKFNDRAMGKLIDITAITPTPLGEGKTVTTIGLCQGLGKIGKKVITTLRQPSMGPVFGIKGGAAGGGYSQVVPMEDINIHFTGDIHAVEAANNLLAAMIDTSILLGNPLNIDPMTVMWNRVLDTNDRALRDIVVGLGGKENGYPRQTSFDMAVASEVMAILALAENLHDLRQRLGRIIVAYTYDGKPVTAEDLKAAGAMTVIMKEALKPNLVQTLEGQACIMHAGPFANIAHGNNSVLADKIALNLADYVVTESGFGSDLGMEKFMDIKCRQ... | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate
Sequence Mass (Da): 60771
Sequence Length: 567
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 6.3.4.3
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Q8RHF4 | MTDIQIAQAAKKENIVEIAKKLGLTEDDIEQYGKYKAKVNLDVLQKNKRPNGKLILVTAITPTPAGEGKSTVTIGLTQALNKMGKLSAAAIREPSLGPVFGMKGGAAGGGYAQVVPMEDINLHFTGDMHAIGIAHNLISACIDNHINSGNALGIDVTKITWKRVVDMNDRALRNIVIGLGGKANGYPRQDSFQITVGSEIMAILCLSNSITELKEKIKNIVIGTSVTGKLIKVGDFHIEGAVAALLKDAIKPNLVQTLENTPVFIHGGPFANIAHGCNSILATKMALKLTDYVVTEAGFAADLGAEKFIDIKCRLGGLKP... | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate
Sequence Mass (Da): 58321
Sequence Length: 544
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 6.3.4.3
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Q5V5Y2 | MEPIWELVEPWGLGLDDLQYFGEYTAKVKQHAIERLREQAENREQNLVLVTGMTPTPKGEGKTVTTVGLGQTLNHVGEEAMIAIREPSLGPVFGVKGGAAGGGRSQVLPMEDINLHFTGDLHALTSAHNLIAAMLDAKISQGDDLNIDINNVSWPRAIDMNDRALRETVVGLGGKTGGTPREDSFILTAASELMAVLCLASDIGDLKERVSRIIVAYDEDGDPVTVEDIEATGPATMLLRDAIKPNVVQTIEGTPALVHGGPFANIAHGTNSLVADKTAFGMGDYLVTEAGFGSDLGAEKFMDVVCRKGDMTPNAVVLVA... | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate
Sequence Mass (Da): 59251
Sequence Length: 553
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 6.3.4.3
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A9B4H8 | MKTSLQIAAEATPRPITQIAEELAIAEQFVEPYGRYRAKINLDLLDASHDRPRGKQILVTAMTPTPLGEGKTATTIGLGMALSRLGKRAICTLRQSSLGPVFGIKGGGSGGGYSQVIPLEDSLMHLTGDIHAVTQAHNQIAAMTDNSWYQKNRLGIDPEQIQIRRVLDVNDRFLRSITIGQGGSQHGIPRQTGFDITAASELMAILALVSGENHADVMRDLRQRIGRMVVAFTRQGQPITADDIQAAGAATVIMRNAIHPTLMQTIENTPVLMHGGPFANIAHGNASVVADQVGLRIADYVVTEAGFAMDMGGEKFFDIK... | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate
Sequence Mass (Da): 60778
Sequence Length: 570
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 6.3.4.3
|
Q1GA94 | MVKSDIEIAQAAEELPITDVAAKLGLTSQDLEPYGYDKAKVNWQAIKRSEENGHLGKLILVTSISPTPAGEGKSTMTIGIGDAINNQLGKKTVIALREPSMGPVFGMKGGAAGGGYAQVIPMEDINLHFTGDMHALTSAIDNLSALVDNYIYQGNELGLDPEKIVIKRGLDVNDRTLRKVTIGQGSKFNGVERPASFQLTVGHELMAILCLSKDIADLKERIGKVLVGYTYEDEPVFVKDLGFQGAIAALLSTALKPNLVQTLEHTPAFVHGGPFANIAHGNNSILSTNLALHLSDYVLSEAGFGSDLGGQKFLDFVSTK... | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate
Sequence Mass (Da): 60503
Sequence Length: 559
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 6.3.4.3
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Q9KLX7 | MLPDIEICRATPLAPIDTIAQKAGLHANEYESHGQHKAKVSLHCLERLANKPKGKFILVTAITPTPLGEGKTVTTIGLAQGLAKLNHSVMACIRQPSMGPIFGVKGGAAGGGYSQVAPMEELNLHLTGDIHAVTAAHNLAAAAIDARIYHEQRLGYADFERRTGMPALRIDPKQVIWKRVMDHNDRALRMVTVGRNEPGKNINGYEREDGFDISAASELMAILALASDLRDLRRRIGNVVLAYDLDGNPVTTEDLKVAGAMAVSMKEAIEPTLMQTLEGVPTLIHAGPFANIAHGNSSIIADEIATRLADYTVTEGGFGS... | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate
Sequence Mass (Da): 62074
Sequence Length: 582
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 6.3.4.3
|
A1JMA3 | MTPTLSSSADVLPSLSNMSSETNLLPIQQIAPQLGLSADDLIPYGHHMAKVDISALRPSGPQGKLILVSSITPTPLGEGKTVTTIGLSQGINRLGYRGVACIRQPSLGPVFGVKGGAAGGGAAQVLPMEKLNLHLTGDIHAISAAHNLAAAALDARLYHEQRLGAVFSQQTGMPLLNIDAQQILWPRVVDHNDRALRHIQVGVGGGTHGVERHDHVEITAASELMAILALSESLHDMRQRIGRIILAHSTSGQAITADDLGVAGAMTALMKETIHPTLMQTSEQTPVLIHAGPFANIAHGNSSVLADRLGLQLADYVVTE... | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate
Sequence Mass (Da): 61470
Sequence Length: 585
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 6.3.4.3
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Q9FL59 | MAAKDGAKSQEDYKLKDMKPELGERWPHGGQRGGTGWIGSERAASTYDLVEQMFYLYVRVVKAKDLPPNPVTSNCDPYVEVKIGNYKGKTKHFEKRTNPEWNQVFAFSKDKVQSSTVEVFVRDKEMVTRDEYIGKVVFDMREVPTRVPPDSPLAPQWYRLEDRRGESKKRGEVMVAVWLGTQADEAFPDAWHSDASSVQGEGVQSVRSKVYVSPKLWYLRVNVIEAQDVEPSDRSQPPQAFVKVQVGNQILKTKLCPNKTTNPMWNEDLVFVAAEPFEEQFFLTVENKVTPAKDEVMGRLISPLSVFEKRLDHRAVHSKW... | Function: Involved in the export of FT from the phloem companion cells to the sieve elements through the plasmodesmata . Regulates flowering time under long days . May function as a signaling molecule by regulating the trafficking of other regulators .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): ... |
Q69T22 | MTMTGGHHHDAHHEDFQLKDTNPLLGEQWPKGAAGPARPAVGGGIAGWLGLEKPSSTYDLVEQMFFLYVRVVKAKDLPPNPITGSPMDPYVEVKLGNYKGTTKHYDRRANPEWDQVFAFSKSRVQSNVLEVYLKDKEMLGRDDYVGRVVFDLAEVPTRVPPDSPLAPQWYRLEERRVGGGGDGGGLKVRGELMLAVWIGTQADEAFPEAWHSDAATVRGEGVASVRSKAYVSPKLWYLRVNVIEAQDVQPQARGRAPEVFVKAQVGNQILKTSVVAAPTLNPRWNEDLVFVVAEPFEEQLLLTVEDRVTPRKDDLLGRAA... | Function: Involved in the export of the long day-specific flower-promoting signal (florigen) RFT1 from the phloem companion cells to sieve elements . Promotes flowering under long days through the transport of RFT1 from the leaves to the shoot apical meristem (SAM) .
Location Topology: Multi-pass membrane protein
Seque... |
Q9C8H3 | MQRPPPEDFSLKETKPHLGGGKVTGDKLTTTYDLVEQMQYLYVRVVKAKELPGKDLTGSCDPYVEVKLGNYRGTTRHFEKKSNPEWNQVFAFSKDRVQASYLEATVKDKDLVKDDLIGRVVFDLNEIPKRVPPDSPLAPQWYRLEDGKGQKVKGELMLAVWFGTQADEAFPEAWHSDAATVSGTDALANIRSKVYLSPKLWYLRVNVIEAQDLIPSDKGRYPEVFVKVIMGNQALRTRVSQSRSINPMWNEDLMFVVAEPFEEPLILSVEDRVAPNKDEVLGRCAVPLQYLDKRFDYRPVNSRWFNLEKHVIMEGGEKKE... | Function: Required for proliferation and differentiation of shoot stem cells in the shoot apical meristem (SAM), thus determining the appropriate balance between the maintenance of shoot stem cells and their differentiation into other aboveground plant parts via the control of subcellular localization and intercellular... |
Q60EW9 | MMQRPFRPEEYSLKETSPHLGGGAAGDKLTTTYDLVEQMQYLYVRVVKAKDLPSKDITGSCDPYVEVKLGNYKGTTRHFEKKTNPEWNQVFAFSKERIQSSVVEIIVKDKDFVKDDFIGRVLFDLNEVPKRVPPDSPLAPQWYRLEERNGHKVKGELMLAVWMGTQADEAFPEAWHSDAASIPGDGLASIRSKVYLTPKLWYLRVNVIEAQDLIPNDRTRFPDVYVKAMLGNQALRTRVSPSRTLNPMWNEDLMFVAAEPFEEHLILSVEDRIAPGKDDVLGRTIISLQHVPRRLDHKLLNSQWYNLEKHVIVDGEQKKE... | Function: Promotes nuclear translocation of the transcription factor OSH1, which directly suppresses the auxin biosynthetic gene YUCCA4 during the late development of anthers . Reduction of auxin levels at late stage of anther development, after meiosis of microspore mother cells, is necessary for normal anther dehisce... |
Q4WAW7 | MPPAPPDQKPCHQLQPAPYRALSESILFGSVDEERWWHSTAPILSRLLISSNYDVDVQYKYLSLYRHLVLPALGPYPQRDPETGIIATQWRSGMVLTGLPIEFSNNVARALIRIGVDPVTADSGTAQDPFNTTRPKVYLETAARLLPGVDLTRFYEFETELVITKAEEAVLQANPDLFRSPWKSQILTAMDLQKSGTVLVKAYFYPQPKSAVTGRSTEDLLVNAIRKVDREGRFETQLANLQRYIERRRRGLHVPGVTADKPPATAADKAFDACSFFPHFLSTDLVEPGKSRVKFYASERHVNLQMVEDIWTFGGLRRDP... | Function: Brevianamide F prenyltransferase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities . The biosynthesis of fumitremorgin-type alkaloids begins by condensa... |
Q4WAW5 | MKPSHSDTPLMMPSVMKCGYLATAGLIGICTHLSYFRYGEHHLYPWRYVRFHLCLTMGVAALLYAKKPPQYTLCSMDLVKDVSLLMATYLVGLFASLLLYRTLFHPLRQIRGPWAAKISSFWLSFRLRRGPSFRILHELHEEYGPVVRVGPSEVSIIHPEAVRMIYGPNSRCSKNTFYDNGHPMMSLHSYRDRIAHDQRRRVWSAGFGDRALRGYEQRMRVYRQKLFQRLEARAVAESAINISQWFNFYSYDTMGDLAFARSFDMLDASRNHWAVDMLMHGMIGYRYLFPSWFFRLLATMPSLSSDWHKFIGFATDTMLR... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities . The biosynthesis of fumitremorgin-type alkaloids begins by condensatio... |
Q9FIM2 | MTSIELLSPLIHDKFRFSTCCSTSSLLYLHASSFFRDRSFGFRQNPNRFVSNSSIQLPQSVPGSINQERFNLWQGFSRKKSTSSSRTIVNCQEGDQKASSSEGEGKTNKDKGRKQGKNELWWSKGKKWQWKPIIQAQEIGVMLLQLGIVMFVVRLLRPGIPLPGSEPRTQTTFMSVPYSDFLSKVNNDEVQKVEVDGFHVLFKLKDDGNLQESETSSSSIKLSESSETMLRSVAPTKRVVYSTTRPRDIKTPYEKMLENNVEFGSPDKRSGGFFNSGLIVLFYIAVLAGLLHRFPVNFSQSTTGQLRTRKSGGPGGGKVS... | Cofactor: Binds 1 zinc ion per subunit.
Function: Probable ATP-dependent zinc metallopeptidase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 87838
Sequence Length: 806
Subcellular Location: Plastid
EC: 3.4.24.-
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A2ZVG7 | MSALQASLLLRPLPSPLPPRRRLPLPSSSASFPRAGHHRRLPLPLRALASEGPQPAPSPAPDPPPPELPAAPEAEEVVGTAAAEGGGKVEEEELEDLVEKGRAWVLALAAAVVAAARRFFDWVVSGDWMSWWPFWRPDRRLQRLIDDADANPADPAKQSALLHELNKFSPEDVIKRFEQRSHAVDSRGVAEYLRALILTNGIADYLPDEQSGRSASLPALLQELKQRVSGNEDKPFMNPGISEKQPLHVVMVDPKATGRSTRFAQEIFSTVLFTIAVGLMWVMGAAALQKYIGSLGGIGASGVGSSSSYSPKELNKDIMP... | Cofactor: Binds 1 zinc ion per subunit.
Function: Probable ATP-dependent zinc metallopeptidase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 85793
Sequence Length: 784
Subcellular Location: Mitochondrion membrane
EC: 3.4.24.-
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Q8VZI8 | MIFSKLGSSLARSSRSKGFVYGGGVRSAVFNQGRLRAPQNLEAAVNQVDGGLGFLRRHFASFAARKGLEAGDLSRAFANPRLRRFFSSQTPKKKNYENYYPKDSKKAPKNEQKSESRDGSKKNENENAGDAFSNEYQNMLIPLMAIALILSTFSLGSREQQQISFQEFKNKLLEAGLVDHIDVSNKEVAKVYVRSSPKSQTTEEVVQGPGNGVPAKGRGGQYKYYFNIGSVESFEEKLEEAQEAIGVNSHDFVPVTYVSETIWYQELLRFAPTLLLVATLIFGARRMQGGLGGLGGPGGKAGRGIFNIGKAQITRADKNS... | Cofactor: Binds 1 zinc ion per subunit.
Function: Probable ATP-dependent zinc metallopeptidase. Involved in the assembly and/or stability of the complexes I and V of the mitochondrial oxidative phosphorylation system.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 89555
Sequence Length: 813
Subcell... |
Q9FGM0 | MSSSTLQASLFLRPPLHTSSFKLYPCLFSSSSLSFCPQSLSSFYRLSSVLHNSRFRPLPCSLRQDNVASDSDFIPKDSAFEVTDSAESNRLVSDTEVSELETNDRFVGGEETKSGGEEAEVSNGVTEGKEEDQKKSKFRIVVLMMALWAAIKRAIEKVMEWEWLSWWPFSRQEKRLEKLIAEADANPKDAALQGALLAELNKHIPEAVVQRFEQREHTVDSRGVAEYIRALVITNAISEYLPDEQTGKPSSLPALLQELKHRASGNMDESFVNPGISEKQPLHVTMVNPKVSNKSRFAQELVSTILFTVAVGLVWIMGAA... | Cofactor: Binds 1 zinc ion per subunit.
Function: Probable ATP-dependent zinc metallopeptidase. Involved in the assembly and/or stability of the complexes I and V. Involved in thermotolerance but not in high light stress resistance or in the assembly/stability of the complexes I and V of the mitochondrial oxidative pho... |
Q9SAJ3 | MEIAISYKPNPLISSSTQLLKRSKSFGLVRFPAKYGLGATRKKQLFRVYASESSSGSSSNSDGGFSWVRLAQSIRLGAERIGEKIGESVKTEIGFDSEEASGRVNEYVARVKDSVHKGHHELTRFKNETVPSFIDWNKWEHWKDIRNWDGKRVAALFIYAFALLLSCQRVYVAIQAPRVERERRELTESFMEALIPEPSPGNIEKFKRNMWRKATPKGLKLKRFIEAPDGTLVHDSSYVGENAWDDDLETTEGSLKKIIGRNARIQTEAKKKLSQDLGVSGEIGDSVGNWRERLATWKEMLEREKLSEQLNSSAAKYVVE... | Cofactor: Binds 1 zinc ion per subunit.
Function: Probable ATP-dependent zinc metallopeptidase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 115105
Sequence Length: 1008
Subcellular Location: Plastid
EC: 3.4.24.-
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A8ZNZ4 | MPIETEPNRTRKNFEPKRFGGSLFILFTLLLFLNLFVLRGPRFPITAYSDFITQVEAGQVERVEVRPDRIRYILKSDQYGFNEGTETAAVFDTVPVGIDLELPKFLREHDVQYFAPPPSSLSWLPTLLGWVVPPLIFFGIWSWLINRNQGAGPAALTVGQSKARIYSEGSTGVTFDDVAGVEEAKTELLEIVDFLAHADKYTRLGAKIPKGVLLVGPPGTGKTLLAKAIAGEAKVPFFSISGSEFIELFVGIGAARVRDLFEQAKQQAPCIVFIDELDALGKARGGPGGFTGGNDEREQTLNQLLSEMDGFDPNVGVILL... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71566
Sequence Length: 655
Subcell... |
A9NE17 | MNKQQKPKRSPLRPDYLVIVIIILLAIGMYFFFTEMMAPKVKQFDEFEFIAAIESGQIATVRSEYVGGDNFNLWEVTGTFTTGNAPEGVGSYVIILYGDRLNNIQDIIITYNELNPSTPITVSFVPHVSVDFWNIISTLLLIAAPIVLVVIMFRSMSSQSNKAQDFTKNRAKLSQGRKVKFSDIAGADEEKAEMAELIDFLKNPKKYADMGARVPKGVLLVGQPGTGKTLLAKAVAGEAQVPFFSISGSDFVELYVGVGASRVRDLFKVAKQSAPCIIFIDEIDAVGRQRGAGMGGGNDEREQTLNQLLVEMDGFSANLG... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70955
Sequence Length: 641
Subcell... |
A0LR74 | MSREVTSGLPQDKPTGSAPPPPPPWRRWLLPIGLLVSLVLLFTFPMRPSSGKTLTYSEFLTALHHHDIKTITIHSDGEASGQFADGRPYSTTIPIGLAGSQLLNELENNGVQISARPPGPSLASQVLAGVLSFLPFLLLLGLFAYSGRRAGAGFLAGLPGIGRARAKIFTTERPQTRFSDVAGYDGVKAEIAEVVDFLRSPERYRRAGAAIPRGVLMVGPPGTGKTLMARAVAGEAGVPFLSVTGSSFVEMFVGVGASRVRDLFEEARKHAPCIVFVDEIDAIGQRRAGAGTIVANDEREQTLNQLLAEMDGFEPAQGVV... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71287
Sequence Length: 666
Subcell... |
C1F8X6 | MNSTVKTIVFWVFILACCILLWQVFQRSSNTGKEQEISFSQFLNDAQQGQIHDVTVVGGEVHGHFRSANAAFHVEVPTNYPQLYDILNKNHVAVTVKDNSGSPWWSILIQFSPVLVLVALWFFMIRQMQSGGNKALSFGKSRARLLSMQQKKVTFKDVAGVDEAKEELKEIIEFLREAQKFQKLGGRIPKGVLLVGPPGTGKTLLARAVAGEANVPFFSISGSDFVEMFVGVGASRVRDLFEQGKKNAPCIIFIDEIDAVGRHRGAGLGGGHDEREQTLNQLLVEMDGFEANDGVILVAATNRPDVLDPALLRPGRFDRR... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70328
Sequence Length: 639
Subcell... |
C7M0M0 | MMPSSQRPSPRGSRQSPSPDQRGRIAFAILATLVVAVLLLTLFSHAPSGQPLGYSTFIHDVQAKQVRTAVLNNTTGQITGSLTNGTAYSVTGPLPYTSSELSTLSKAHVQVSYITPGPGIASTIIEYVIFFGIFIGIWVYLTRRTQGSVNGIMSVGRSRAKTYTTERPKTTFDDVAGYQGVKGEVKEVVDFLRDPSRFSQLGARIPKGILLVGPPGTGKTLLARAVAGEAGVPFMSVSGSDFMEMFVGVGAARVRDLFQTARRQSPSIIFIDEIDSIGRKRGTGLGGGHDEREQTLNQMLSEMDGFDPAEGIVVMAATNR... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71888
Sequence Length: 660
Subcell... |
B2UMY1 | MPPSPPRPPKFPGSGRPESPNWGVWVMVLLIVGVLAFGFFTPESFGLGPRKENLESFEAQYKAGRVVLNDPKAPVEVVLSENGSEGVIHALVYRKEIQPKVEMTPFALTYSMSLPDRDKPLLNELSGYRVVESPYRTEEGKNVSLIPEGAQKLSVPEFNRLALEGRIAGGKDGIILAEDGNQNVLVGQIVTRIWPAATGDASVDKQRFERVEVPFTLEFQGDRVKQLLGPDTKFKRESGSWGGILLNLLPIVLILVILFFMFRAQSGGARGAMSFGKSRARLISPDKNKVTFKDVAGISEAKEEVWELVEFLRNPEKFRD... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 89455
Sequence Length: 812
Subcell... |
P94304 | MNRIFRNTIFYLLIFLVIVGIVSVFNSDQTETENVSFNEFAERLENGQVQELSVKPERQVYLVRGQFNDQAEDEFFQTYALRSEQTAELLFNAEDPTGTPFNLEIEPADETSGWVQFFTGIIPFIIIFILFFFLLSQAQGGGSRVMNFGKSKAKMVNEDKKKAKFKDVAGADEEKQELVEVVEFLKDPRKFSAIGARIPKGVLLVGPPGTGKTLLARAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFENAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFSANEGIIIIAATNRADILDPA... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75446
Sequence Length: 679
Subcell... |
B8J992 | MSADEKKGHGQRSERGRGPGGPGTQPRIPLASPAAWLVLIALAIFLFRAFQDVGVRRIPYSQFKEMVRQSAFERVVIGPDWVRGVPKPVEAGAAQGGGAQPQQQAQGEGERNGQALPYVATRIPGGGDDLVQAVEKAGVPYDAVAGGGMGDLFWVWIAPIAIGLLFWAWVMRRMSGQLGQGPPGVMAFGKSRARIHMEPDTGVTFQDAAGIDEAVEELQEIVEFLKTPEKYRRLGGRIPKGVLLVGPPGTGKTLLARATAGEAGVPFFSLSGSEFVEMFVGVGAARVRDLFAQATQKAPCIVFIDELDALGKSRNAGIMG... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 76249
Sequence Length: 706
Subcell... |
O67077 | MNALKNFFIWAIIIGAAIVAFNLFEGKREFTTKVSLNEVVKLVEEGKVSYAEVRGNTAIIQTKDGQKLEVTLPPNTNLVDKMVEKGVRVEVANPEPPGGWLVNVFLSWLPILFFIGIWIFLLRQMSGGGNVNRAFNFGKSRAKVYIEEKPKVTFKDVAGIEEVKEEVKEIIEYLKDPVKFQKLGGRPPKGVLLYGEPGVGKTLLAKAIAGEAHVPFISVSGSDFVEMFVGVGAARVRDLFETAKKHAPCIIFIDEIDAVGRARGAIPVGGGHDEREQTLNQLLVEMDGFDTSDGIIVIAATNRPDILDPALLRPGRFDRQ... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70686
Sequence Length: 634
Subcell... |
Q2NIN5 | MSFFDKIFKKFHMGVLYFAVILIGATFIYCYFTKHEKKDNNTFDALAQKNEIEKIQYNPIFANSAFCDIVVTTTDGRVIDFFNIPYDKVFEKKPNGKYKYNTYSVDPRPWNGYEHVFWVFRQCLTMLFFYCFFLFFADTIKQMGQEILASTSGKKGAKSRKVIINHKRFTFSDVAGADEEKEEMSELIDFLKNPRKYAAMGARIPKGVLLYGPPGTGKTLLAKAVAGEAGVPFFAASGSDFDEVYVGVGASRVRDLFKEAQLAAPCIVFIDEIEAVARKRGSNIGGSNGSEQTLNQLLVEMDGFNQKMGVIVIAATNQPE... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75765
Sequence Length: 676
Subcell... |
P37476 | MNRVFRNTIFYLLILLVVIGVVSYFQTSNPKTENMSYSTFIKNLDDGKVDSVSVQPVRGVYEVKGQLKNYDKDQYFLTHVPEGKGADQIFNALKKTDVKVEPAQETSGWVTFLTTIIPFVIIFILFFFLLNQAQGGGSRVMNFGKSKAKLYTEEKKRVKFKDVAGADEEKQELVEVVEFLKDPRKFAELGARIPKGVLLVGPPGTGKTLLAKACAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFENAKKNAPCLIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFSANEGIIIIAATNRADILDPALLRPG... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70937
Sequence Length: 637
Subcell... |
O83964 | MERSPLPRIIALTFGTLLFVSAVLLTLSTFLPLFTLHRASHWFFVPGTLLYETYAFSSLLVPLLLLHTALLLFVGGRSLRAESALVAFPLLFITAVCGEHGLYALRRALAARSISPSTRGGIDIVCVLCLLALLGAELYAALIYGERCYVWFHARIPRDFIADGFQDPSFPPSTADHPDTVSPPPAPSCATADVQTPEASAPPEGQFSTEVPLQGGEFLISEAEVQPATQVAACGGVSTPTALAPSVPSQAPFPLLPAPGLIQSNLPSDVHAPASPGSLPSVIPAQAPCVMALSPISAPSVAPAETLIPAQDDEQGPPRP... | Function: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the ... |
Q83MS8 | MSAKKSYLKVWRGLAGAAGSCARVFSKKSLARRDRRDQLPFALFLFGLVGAVFQWFLYGNWLSGIVSEYTVAAFFGGFSIVLPILLIGFSIWLFRNPQKTHDNIRVSIGLFMFSSFSAAFLHFSAGFPYPSSGIRILSTAGGIIGWLVGLPLTTLPSYLAKTVCIIFIVLSVSVISKTPISKIVRVIFRYAKWLFNSDSVKTSPNSSVSSSSEHQELTGRDMPDTAGDNRHDETVTVLSGTSLTGSPVSEYHGESSDYALPSLDILNSYPPAKHDDAENEKVITALSGVLRQFSVNARFSGFSRGPTVTQYELELGEGVK... | Function: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the ... |
Q84I33 | MFKENKNKVETIIKTSEEAPSSRLNGSQRLKESGLILAFLFSIFLAVALFSFNPADPSWSQTAWGTDIHNAGGLVGAWLADTLFFVFGSLAYPLPFITAFAAWVLLRKRDEGDEIDFTLWGTRLLGLTIVLLTSCGLADINFDDIWYFSSGGVIGDVLTSLALPTLNILGTTLVLLFLWGAGITLLTGISWLRIVEWIGERSIAAFVGLFNRLRGEKAERVKPALVKPELPVEELEPTFSASMDTEIDEPAPSLRRFNIHMPEERDVPDIHFEPQVEPKVELKPEPPRQREPAPHFSRVAAQNTQVEPVSSARTQQWDAT... | Function: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the ... |
Q8D8M2 | MFKENAKKVQTIIKTSEEAQSSRLNGFQRLKECCLILGVLTSAFLSIALLTFSPADPSWSQTSWGGDISNAGGQFGAWVADTLFFTFGLLAYLLPVLLVIVTWVFFRTRDEDEHIDLMLWGTRLLGLAILILTSCGLADINFDDIWYFSSGGVLGDVLNSLALPTLNLLGTTLVLLFAWGAGFTLLTGISWLSIVEWIGSLFLDVCQWALNRLRGEKTEVIAPELQPIALSDDEPKAQPQIEAQQDEIVEEERIPDPLPVEPVVQMRREYPIHMPQTVSYQTVSDELDELEDNSFERAKKLNATIEELEQEALSVNDLPD... | Function: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the ... |
Q8P993 | MAKQVPERSKPAEGKSSSRKPAAADTPRRQKLWRDLALIAVAPLLLYLLASLFTYSAADPGWSQTGSVVAPVHNMGGRVGAWIADVLLQLFGYVAFLLPVVLGAVAWIALFGMDKEGQAEADLGPALRLVGMVGFLIASTGFLHLRLFNGDVAGAGGILGRLVSNSLSAGFGALGANLFVVVLLLVSITLATGLSWFVVMERIGKWVLALGPLLQRKSHQATEWQQTRVMREEREEVRKVDAVKQAKREPVKIEPPPAPVVEKSERAKRDTQIPMFQGVSTDGSDLPPLALLDDPKPQAKGYSEETLETLSRQIEFKLKD... | Function: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the ... |
Q81WC4 | MSNLAVKYKQQAQEEVQIQTPPQQMVQPKAKAKITRIEKLLYVAFIGFLLYACVAFIGNKAGLYQVNVEAATIEQKIVQQQKENQELQAEVEKLSRYERIAEVAKKHGLEINANNVKGLK | Function: Essential cell division protein.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 13601
Sequence Length: 120
Subcellular Location: Cell membrane
|
Q07867 | MSNLAYQPEKQQRHAISPEKKVIVKKRASITLGEKVLLVLFAAAVLSVSLLIVSKAYAAYQTNIEVQKLEEQISSENKQIGDLEKSVADLSKPQRIMDIAKKNGLNLKDKKVKNIQE | Function: Essential cell division protein that may play a structural role. Probably involved in the regulation of the timing of cell division. Also required for sporulation.
PTM: Cleaved by RasP. Cleavage is important for turnover and function of FtsL.
Location Topology: Single-pass type II membrane protein
Sequence Ma... |
Q7VUP7 | MGRISLIVAALLMLSAISLVTSRYQSRQLFIELGRSQAEARDLDTNWRRLQLERAELARNARIDRAARDDLKMIPIVPDRTLYMNQPAGGAQ | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 10438
Sequence Length: 92
Su... |
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