entry
stringlengths 6
10
| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
|
|---|---|---|---|---|
W4VS15
|
ICK30_TRILK
|
U16-barytoxin-Tl1c (U16-BATX-Tl1c) (Toxin ICK-30)
|
MKTIIVFLSLLVLATKFGDANEGVNQEQMKEVIQNEFREDFLNEMAAMSLLQQLEAIESTLLEKEADRNSRQKRCNGKNVPCGSNHSPCCSGLSCEETFGYGWLYKSPYCVIPSNG
|
Ion channel inhibitor.
|
W4VS20
|
ICK25_TRILK
|
U16-barytoxin-Tl1a (U16-BATX-Tl1a) (Toxin ICK-25)
|
MKTIIVFLSLLVLATKFGDAKEGVNQEQKKEVTQNEFRVEYLNEMAAMSLLQQLEAIESALFEKEAGRNSRQKRCNGKNVPCGANHSPCCSGLSCEETFGYGWLYKSPYCVIPSNG
|
Ion channel inhibitor.
|
W4VS23
|
ICK20_TRILK
|
Toxin ICK-20
|
MMKYFLVLCLVVLGVAAVQAAALEDEKFLNLAESLAMPEESRCKARRYGCTDKAECCSEKCAYPALTCAFNWSCEKVCA
|
Ion channel inhibitor.
|
W4VS32
|
TX21F_TRILK
|
Toxin ICK-15
|
MKPIVSILIFCALAVVIMGHPLDSGYGIPHIVEKLPNGQWCKTPGDDCSKSNECCKPKDPENYSGGCVAQWSGMHGKRINMCRICYLESSMC
|
Probable neurotoxin with ion channel impairing activity.
|
W4VS46
|
ICK10_TRILK
|
Toxin ICK-10
|
MMKLYSLVIIATLAAAAFAATKQEIAAAALSGMVHDFEQYAKRAEGEEEPKRYIRCSKQLGEKCDLNCECCGASAVCEDYNYICKEKVSDNPVLDWFGQGLNAMGNAISRYYCDAE
|
Ion channel inhibitor.
|
W4VS49
|
ICK5_TRILK
|
U11-barytoxin-Tl1b (U11-BATX-Tl1b) (Toxin ICK-5)
|
MKTLVLVAVLGLASLYLLSYASEVQQLSRDEEEFRALVASFGGLFDTEERGVDKEGCRKLFGGCVGDGDCCLHLGCKTRKLPPFADPYCAWDWTFGRK
|
Ion channel inhibitor.
|
W4VSA2
|
ICK39_TRILK
|
U17-barytoxin-Tl1a (U17-BATX-Tl1a) (Toxin ICK-39)
|
MKTIIVFLSLLVLATKFGDANEGVNQEQMKEVIQNEFREDFLNEMAPMSLLQQLEAIESTLLEKEADRNSRQKRCLGENVPCGDFPCCGKLVCQKTFGYGWLYKSPYCVKPSNG
|
Ion channel inhibitor.
|
W4VSA5
|
ICK34_TRILK
|
U16-barytoxin-Tl1f (U16-BATX-Tl1f) (Toxin ICK-34)
|
MKTIIVFLSLLVLATKFGDANEGVNQEQMKEVIQNEFREDFLNEMAAMSLLQQLEAIESTLLEKEADRNSRQKRCNGENVPCGPNHSTCCSGLSCEETFGYGWWYDTPFCVKPSKG
|
Ion channel inhibitor.
|
W4VSA7
|
ICK29_TRILK
|
U16-barytoxin-Tl1e (U16-BATX-Tl1e) (Toxin ICK-29)
|
MKTIIVFLSFLVLVLATKFGDANEGVNREQTKEVIQNEFRGDFLNEMAAMSLLQQLEAIESALLEKEADRNSRQKRCNGNNVPCGPDHPPCCSGLSCEETFGYGWWYKSPYCVRPSKG
|
Ion channel inhibitor.
|
W4VSB0
|
TX33C_TRILK
|
Toxin ICK-24
|
MKLFMVLVASFAFAVALPSKKREETAAENELTGDLQEAAQPMIYAVAFPEIRASCVIGWKQQGATCQRDCECCGVAATCITGDSSTGFCGYHQTPNALGQGILYTADTIKNGFSAIFCAG
|
Ion channel inhibitor.
|
W4VSB2
|
TX21J_TRILK
|
Toxin ICK-19
|
MKPIVSILIFCALAVVIMGHPLDSGYGIPHIVEKLPNGQWCKTPGDDCSKNNECCKPKDPENYSSGCASQWSGMQGKRVNMCRICYIESSMC
|
Probable neurotoxin with ion channel impairing activity.
|
W4VSB6
|
H71_CONVC
|
Conotoxin Vc7.1 (H_Vc7.1)
|
MNTAGRLLLLCLALGLVFESLGIPVADDVEAVRDTDPDEKDPSVHNSLKAVYGDCGGERCRFGCCKTDDGEEKCQHFGCP
|
Probable toxin with unknown function (Probable).
|
W4VSB7
|
ICK14_TRILK
|
Toxin ICK-14
|
MKPIVSILLFCALAVVIVGRRRSTGRGIPYVDEKLPNGQRCKPPGFDCSKSEECCGPQDTKNYAHGCAPQWSGMWNKRVNECYICYIESSSC
|
Probable neurotoxin with ion channel impairing activity.
|
W4VSB9
|
ICK9_TRILK
|
Toxin ICK-9
|
MMKLYSLVIIATLAAAAFAATSEEISAAVSEIISQHQQDLERYAKIVERGEEPKKYIRCSKQLGEKCDLNCECCGAAAYCEDIVYICKEKISDNSILNAFGQAMTAMGNAVSRYYCDAE
|
Ion channel inhibitor.
|
W4VSC0
|
ICK4_TRILK
|
U11-barytoxin-Tl1a (U11-BATX-Tl1a) (Toxin ICK-4)
|
MKTLVLVAVLGLASLYLLSYASEVQQISRDEEDFRALMASFGGIFDTEERGVDKEGCRKMFGDCWGDGDCCLHLGCKTRKLPPWTDKPYCAWDWTFGRK
|
Ion channel inhibitor.
|
W4VSC2
|
PE1_TRILK
|
Peptide 1 (Prokineticin-1)
|
MNVLLLMCAVTLMVCVSSETYCGSQLCGEGYCCTGGHFRRQCRPLADEGQQCEKENKYNDYKLGCPCKGGMICSDIKYCQKL
|
Non-toxic to mice and insects.
|
W4VSG7
|
CH1_CONVC
|
Conotoxin Vc1 (H_Vc1)
|
MRTSGRLLLLCLAVGLLLESQAHPNADAGDATRDVGSDRTSVELSKMLKGWQAEKGQRKASAPKKFYVYPPVRRSFY
|
Probable toxin.
|
W4VSI1
|
ICK38_TRILK
|
U17-barytoxin-Tl1d (U17-BATX-Tl1d) (Toxin ICK-38)
|
MKTIIVFLSLLVLATKFGDANEGVNQEQMKEVIQNEFREDFLNEMAAMSLLQQLEAIESTLLEKEADRNSRQKRCLGENVPCGDFPCCGKLACEKTFGYGWWYKSPFCVKPSKG
|
Ion channel inhibitor.
|
W4VSI3
|
ICK33_TRILK
|
U16-barytoxin-Tl1f (U16-BATX-Tl1f) (Toxin ICK-33)
|
MKTIIVFLSLLVLATKFGDANEGVNQEQMKEVIQNEFREDFLNEMAPMSLLQQLEAIESTLLEKEADRNSRQKRCNGENVPCGPNHSTCCSGLSCEETFGYGWWYDTPFCVKPSKG
|
Ion channel inhibitor.
|
W4VSI4
|
ICK28_TRILK
|
U16-barytoxin-Tl1d (U16-BATX-Tl1d) (Toxin ICK-28)
|
MKTIIVFLSLLVLATKFGDANEGVNQEQMKEVIQNEFREDFLNEMAAMSLLQQLEAIESTLLEKEADRNSRQKRCNGNNVPCGPDHPPCCSGLSCEKTFGYGWWYKSPYCVRPSKG
|
Ion channel inhibitor.
|
W4VSI5
|
TX33B_TRILK
|
Toxin ICK-23
|
MKLFMVLVASFAFAVALPSKKREETAENELTGDLQEAAQPMIYAVAFPEIRASCVIGWKQQGAKCERDCECCGVAATCITRSTNSLPGFCGYRQTPNVLGQGLLYTADTISNGLSAIFCAA
|
Ion channel inhibitor.
|
W4VSI6
|
TX21I_TRILK
|
Toxin ICK-18
|
MKTIFALVFCCAIAVVVLGFGENEGSTIDHDQNNCKGPGSRCSNKNECCKPKDMETYTYYCGSRWDSSSGDFVRKCVICNRESSMC
|
Probable neurotoxin with ion channel impairing activity.
|
W4VSI7
|
TX21D_TRILK
|
Toxin ICK-13
|
MKPTISILIFFALAVAIMGHRLNSGYGIPHIVEKLPNGQWCRTPGDDCSESKQCCKPEDTATYAHGCSQQWSGQRGELVKMCYICNKESSMC
|
Probable neurotoxin with ion channel impairing activity.
|
W4VSI8
|
ICK8_TRILK
|
Toxin ICK-8
|
MMKLYSLVIIATLAAAAFAATSEEISAAVSEIISQHQEDLERYAKIVERGEEPKKYIRCSKQLGQSCYLNCECCGASAVCEDIKYICKDKVSDNSILDAMGKAWNAVGNSISRYYCSAE
|
Ion channel inhibitor.
|
W4VSI9
|
ICK3_TRILK
|
U10-barytoxin-Tl1a (U10-BATX-Tl1a) (Toxin ICK-3)
|
MKTLVLVAVLGVASLYLLSSASEVQQLSPAEEEFRAFVSTFGGLFETEERGVDSEDCRAMFGGCGEDNDCCLHLGCKTTKLPPFANPYCAWDGTTGRK
|
Ion channel inhibitor.
|
W6JIC6
|
CAPSD_CPBDV
|
Capsid protein (Viral protein 2) (VP2)
|
MARTKSKPRKRTTVRKARRSVKRRTTTKGTKRKTAGDPVTKAKRGVATSSPFAAHHAVRMNPFSGATTQPKIPDGGFTSSLSRRLQNVVEVTNASNEGIMHLVMAPTMGVPICVTHTTEGASTRSGATLKPSYLGFLGQGVGLETKVGGVIKWPIANTDTGDVINAADFAKWRVVSQGLQITLNNVDDENDGWFEAVRFNWRNDNEDICLTSLDGTDTGNVIGAAPNLNGLPLLTANIVEMPGYKSGLLKDIKDYQFMLHPQQTRHDPVEITKSIDFVGGTDLNYDTQSKKANLGDSAAGTLLKQGLVDQNMDWMYIRIHPRSNTGAAGQTGSKLICNYIQNLEFAFSPDSDLATYMTTNRMDPKSAKINDQLNNNQDAANKKREFN
|
Self-assembles to form the virion icosahedral capsid. {ECO:0000255, ECO:0000305}.
|
W6PQG8
|
ABAA_PENRF
|
Conidiophore development regulator abaA
|
MATDWQPECLVAQNQPSLDPVGAHSDRALQNTTGNVQSYSDQLAHAGVTARDDQFHQYSFKYPHGPHPQPLSAPGLHQQHVAARLHQRKLRRLHSVGPNSQSRRAQSSYLKSQKYMEYRRRPRRDTGKDGEPVWSDELEDAFQQALEANPPMGRRKWSERGKSYGRNELIAEYIFKLTGKRRTRKQVSSHLQVLDSFLKGDPDWERLVREPALERSSSVHGSAPAPKWRTAVEHPSGSSHYGSHTHPSYHDHMRSMQPYAGDLPPPHYTLGSNMQETAASTIHGFSFDMWVSAPQQANRIDKALHAYTRLQGDLHHPVAPPMPLEHVNGWRSSFPQLASMVDDVNNPLDCDIILLEVNLELMTDFPPTGSRLGIQLDLDYGHPSAGDVLGVSQMDNWTCSTHIYQDSQKLLETYHDLPKTQSTKVKPLFESSWWAKLFTQLTQEKRIAEDSGNPQAARDADDHARQFFRSLSAVQEIRATSPSSCRLSNQYQGHHGDESKRMAVLAWKFRQTRPGEVGTTTWRRLIPAPDRTTTNSPRPASAVDRVPLSLDSILLNKPSHQGIYQAPHPHDLIHHPSQSQSQWPMYQSPHDNVSNLYNPSGHLDFMSSISKAEDGLNDKIAVTSVLDSFSASLAPESISSTSLHGSSGAPVMLNVHDLPLTHPGMGYTMGHETSHYVPSQHHSVNMHDSNSVLHGFFGSHTQPLDDLSHGHGSWGTHSTSIPGDVGAGSYHIPYQAEHHGPVSRESQQPHQFDGLLPSEDLMDKIVGRMSNGSGMHGAGPDAGYDNATVDAV
|
BrlA, abaA and wetA are pivotal regulators of conidiophore development and conidium maturation (By similarity). They act individually and together to regulate their own expression and that of numerous other sporulation-specific genes (By similarity). Binds to the sequence 5'-CATTCY-3', where Y is a pyrimidine, making both major- and minor-groove contacts (By similarity).
|
W6Q0S4
|
IFGH_PENRF
|
Fumigaclavine B O-acetyltransferase ifgI (EC 2.3.1.205) (Isofumigaclavine biosynthesis cluster B protein I)
|
MSTSFDHSVILSPLDHIAPQAYVSYLLSFQTANSTHCLSLLEAGITRLTKVLPLLLGHIVVNPELDGKYNIQSVQIPCTKEDRTILVHKHHPFPMESALGGVQSGMSMLETSDSKQHLCPLPPLIPSTERQPVIRFQANIFTDAIVLAMTFSHIVFDGTGAAKILALLGRCCRDPSVTPLPLIIDEQDRAQSAIFAGLADTSPAQDHTAELGPAPAIHPVPLDAASLRTCRFEFNSERILQLKYQCSQVLKNACMFQPNSASIPVADLPPFLSSNDVLTSALADAIQRVKSQSKTYDCLDLCMAVNMRGRIELSAAREFLGNMACNLRLKTPGPEYTGPEQCLSCRKTHDCPIQTDQLRFLTDLACKVRNKVRNMDRKYFQSCMTYIANQKDWSQTGMIFTDLAFSSWRHLDIYGLDFGDSFGIVHNFDLSFGLIEGDVIFLPKRLTCDQKEAGWDVHITLPAKDLEALVKDDLIRWLMGRDGE
|
Fumigaclavine B O-acetyltransferase part of the gene cluster that mediates the biosynthesis of isofumigaclavines, fungal ergot alkaloids. The tryptophan dimethylallyltransferase ifgA catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan. The second step is catalyzed by the methyltransferase ifgB that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of N-methyl-dimethylallyl-L-tryptophan. The catalase ifgD and the FAD-dependent oxidoreductase ifgC then transform N-methyl-dimethylallyl-L-tryptophan to chanoclavine-I which is further oxidized by ifgE in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde. The chanoclavine-I aldehyde reductases ifgG and/or fgaOx3 reduce chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline. The festuclavine dehydrogenases ifgF1 and/or ifgF2 then catalyze the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine. Hydrolysis of festuclavine by a yet undetermined cytochrome P450 monooxygenase (called ifgH) then leads to the formation of isofumigaclavine B which is in turn acetylated by ifgI to isofumigaclavine A. Penicillium roqueforti has interestingly at least two sets of genes for the consumption of chanoclavine-I aldehyde on three different loci, the OYEs ifgG/fgaOx3 and the festuclavine synthase homologs ifgF1/ifgF2. The reason for the duplication of these genes is unclear, probably to ensure the conversion of chanoclavine-I aldehyde by differential gene expression under various environmental conditions.
|
W6Q1E9
|
IFGF2_PENRF
|
Festuclavine synthase II (EC 1.5.1.44) (Festuclavine dehydrogenase ifgF2) (Isofumigaclavine biosynthesis cluster A protein F2)
|
MTILVLGGRGKTASRLAALLDQAKTPFLVGSSSASPSDPYKSSQFNWLKRDTWERPFEQAGKHGLGTISSIYLVGPPVMDIAPPMIEFVDLARAKGVQRFVLLSASTVEKGGHSMGQVHAYLDSLAEVEYVALRPTWFMENLLEDPSREWIKNENQIITATGDGKIPFVSADDIASVAFHCLTEWGSHKTEYVILGPELLSYGQVAEILTTILGKKIIHRSLTETGLAELLVKKAGIPADFAAMLSAMEVDVKNGPQEVLNNSVVEVTGNPPRYFKDVAEHEKHVWA
|
Festuclavine synthase part of the gene cluster that mediates the biosynthesis of isofumigaclavines, fungal ergot alkaloids. The tryptophan dimethylallyltransferase ifgA catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan. The second step is catalyzed by the methyltransferase ifgB that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of N-methyl-dimethylallyl-L-tryptophan. The catalase ifgD and the FAD-dependent oxidoreductase ifgC then transform N-methyl-dimethylallyl-L-tryptophan to chanoclavine-I which is further oxidized by ifgE in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde. The chanoclavine-I aldehyde reductases ifgG and/or fgaOx3 reduce chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline. The festuclavine dehydrogenases ifgF1 and/or ifgF2 then catalyze the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine. Hydrolysis of festuclavine by a yet undetermined cytochrome P450 monooxygenase (called ifgH) then leads to the formation of isofumigaclavine B which is in turn acetylated by ifgI to isofumigaclavine A. Penicillium roqueforti has interestingly at least two sets of genes for the consumption of chanoclavine-I aldehyde on three different loci, the OYEs ifgG/fgaOx3 and the festuclavine synthase homologs ifgF1/ifgF2. The reason for the duplication of these genes is unclear, probably to ensure the conversion of chanoclavine-I aldehyde by differential gene expression under various environmental conditions.
|
W6Q4S2
|
ORF7_PENRF
|
PR-toxin biosynthesis cluster protein 7
|
MEPQTKDPDPLPRLVHIGEIQFNLGEVTTGGVTPRGTFIFCPITGGHFTTVFPLPDGFGIHSEAIEGLRAEVLPGGGDYPLIHNNELAELNVSVVAKGLNNDHIFRITSFGICEWNKLIFDMMGQTAAARSTEMGEINAWQVFRINTDSPEYAWLNWACIIGQERLIYEDSRMAKTHMKLFQFLVK
|
Part of the gene cluster that mediates the biosynthesis of PR-toxin, a bicyclic sesquiterpene belonging to the eremophilane class and acting as a mycotoxin. The first step of the pathway is catalyzed by the aristolochene synthase which performs the cyclization of trans,trans-farnesyl diphosphate (FPP) to the bicyclic sesquiterpene aristolochene. Following the formation of aristolochene, the non-oxygenated aristolochene is converted to the trioxygenated intermediate eremofortin B, via 7-epi-neopetasone. This conversion appears to involve three enzymes, a hydroxysterol oxidase-like enzyme, the quinone-oxidase prx3 that forms the quinone-type-structure in the bicyclic nucleus of aristolochene with the C8-oxo group and the C-3 hydroxyl group, and the P450 monooxygenase ORF6 that introduces the epoxide at the double bond between carbons 1 and 2. No monoxy or dioxy-intermediates have been reported to be released to the broth, so these three early oxidative reactions may be coupled together. Eremofortin B is further oxidized by another P450 monooxygenase, that introduces a second epoxide between carbons 7 and 11 prior to acetylation to eremofortin A by the acetyltransferase ORF8. The second epoxidation may be performed by a second P450 monooxygenase. After the acetylation step, eremofortin A is converted to eremofortin C and then to PR-toxin. First the conversion of eremofortin A to eremofortin C proceeds by oxidation of the side chain of the molecule at C-12 and is catalyzed by the short-chain oxidoreductase prx1. The cytochrome P450 monooxygenase ORF6 is probably also involved in this step. The primary alcohol formed at C-12 is finally oxidized by the short-chain alcohol dehydrogenase prx4 that forms PR-toxin.
|
W6QB19
|
ORF10_PENRF
|
Transcription factor ORF10 (PR-toxin biosynthesis cluster protein 10)
|
MFGTLRIGSEKNSVEFIEHAKGEAASRLGGYVFSHSACESCRLKKLRCSGHKSGCDRCRSQAMKCSYQIGAPSNSSRPKSRSHFQPNFSNMSGTAGTSKAPSPLGNDGVDREIGGWEMAETDPTGSVVTTTAQFLNSVNQGEHSNLNDLRQGQRFGGELDYSENELNDIFSNIAYLQPDDMETNVFVGAANRAVLDAEAFDSMTEPANSMSDDIGDIAASQPPSADVQSAFMAFDHARTSSSSSSHQSSDTSASDAFIATDFDGARSRTDPSTCQCRGSILRVLAEIESNILSASPSNMYAILSYLRQTTAASNDILTCRICNCRLKFFGLLGIIGEKITSLSGAIITAFVCRLKEQNESVDFGKSDSPDKRLDPNRAIQLCEFQVQSLQEFKVVSAAVIKLQLKYSVAFVSRTRELAISMNHLAQAQSLEKLESRLNELVIKMQRMVSEVDSDLCDI
|
Transcription factor that specifically regulates the expression of the gene cluster that mediates the biosynthesis of PR-toxin, a bicyclic sesquiterpene belonging to the eremophilane class and acting as a mycotoxin.
|
W6QM20
|
WETA_PENRF
|
Developmental regulatory protein wetA
|
MFAQQYDHSFNDLFNQYVNMETSAADGKDSALSEFDQLFPLDSLSNDCGDLAPTVSTPKCHQSPQPWSNEWSLQYDGPAADHFAFHDTVHPSAISDVNLNHFEVPSRPTATHALSISPSTPPATPRRKPTQSALITPKTIRHRSPNERRSHLRKQSFSPSLMRSSNLSKSRMAYPEAWAQRLQNFSLHNSEDRLPLSPPPSDALIQHENMPTEQIMNQSRDSAEMPPQYDARLYHQSPSVPMQSPSIAMSARQQQHYIAHPSSSALTNSSPSSADDIFSLSHSSDLHSLSSWQSDSLHASSLPFTPDLQGQESQWWSPMPSRVAQQQAAYLASPTPVRHMQNVGSQNDIMQGGLMIQFNPSYDMSADHSFSSNMLPTSSQKFDTSYTSSQVHDISRSSSSLSPKTGTSPRDTHHGSISKPTHRRTHSRKLSSQSMNTPKPAKAPSSSSRGSNKSVSVSFVNFTADDSKKILTGVAPSGSSKTKARREQEARDRRRKLSEAALRAVRSAGGDVEALEAVLC
|
BrlA, abaA and wetA are pivotal regulators of conidiophore development and conidium maturation (By similarity). They act individually and together to regulate their own expression and that of numerous other sporulation-specific genes (By similarity).
|
W6QRI9
|
IFGF1_PENRF
|
Festuclavine synthase I (EC 1.5.1.44) (Festuclavine dehydrogenase ifgF1) (Isofumigaclavine biosynthesis cluster A protein F1)
|
MTILVLGGRGKTASRLAALLDAAKTPFLVGSSSTSQESPYNSSHFNWYEKTTWDNPFAEIGKHGLQPISAVYLVGPPTMDMVPPMIQFVDLACSKGVQRFVLVSASNIEKGDHSMGQVHAYLDSLPGVEYVALRPTWFMENLLEDPQRTWIKNESQVVSATGEGKIPFISADDIASVAFHCLTEWGSHKTEYIIQGPELLSYGQVAEILTSILGKKITHRSLSEAEYTNILVDEIGMPADFAAMSAAMEVDVKNSPQETLNGSVEEVTGNPPRFFRTFAEHEKQKWV
|
Festuclavine synthase part of the gene cluster that mediates the biosynthesis of isofumigaclavines, fungal ergot alkaloids. The tryptophan dimethylallyltransferase ifgA catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan. The second step is catalyzed by the methyltransferase ifgB that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of N-methyl-dimethylallyl-L-tryptophan. The catalase ifgD and the FAD-dependent oxidoreductase ifgC then transform N-methyl-dimethylallyl-L-tryptophan to chanoclavine-I which is further oxidized by ifgE in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde. The chanoclavine-I aldehyde reductases ifgG and/or fgaOx3 reduce chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7-didehydroergoline. The festuclavine dehydrogenases ifgF1 and/or ifgF2 then catalyze the reduction of 6,8-dimethyl-6,7-didehydroergoline to form festuclavine. Hydrolysis of festuclavine by a yet undetermined cytochrome P450 monooxygenase (called ifgH) then leads to the formation of isofumigaclavine B which is in turn acetylated by ifgI to isofumigaclavine A. Penicillium roqueforti has interestingly at least two sets of genes for the consumption of chanoclavine-I aldehyde on three different loci, the OYEs ifgG/fgaOx3 and the festuclavine synthase homologs ifgF1/ifgF2. The reason for the duplication of these genes is unclear, probably to ensure the conversion of chanoclavine-I aldehyde by differential gene expression under various environmental conditions.
|
W6QV39
|
BRLA_PENRF
|
C2H2 type master regulator of conidiophore development brlA
|
MRSHGQHISDRLTVEVDCHSLSSSECPSMTSGFSPLDSPTPTPTSLYSQGSMASPGWHDHPHYHHGVPMERRTSATPLRSAFRMADLTSSETMMGMPCGTMDRQEQMPLPDYLPGYDENVDQLWIPQDMPKTYHEHQFPYQASMPQYNQMARNYYHRPQQAGYLPESASNPCLSRPIFTQPTERMPNSASMSNMLHWMPSHESLVPQTITPAQVQPFPSGPVTPPSSSYSDFPTNIPTFKSHTPSTPHRSVSMGTPSGSDTPVSRMSGHNDYQEDFQLSPVYREGMMQRHRQPSRKSSKKQLLRSNLSLENLPSIIKQVQFKCKEPGCKGRFKRQEHLKRHMKSHSKEKPHVCWVPGCHRAFSRSDNLNAHYTKTHSKRGGRNRYVATLDETSQDFDPDFRGQLTPDGRPIYGSKLEDTMPDCGELSVDGWDD
|
BrlA, abaA and wetA are pivotal regulators of conidiophore development and conidium maturation (By similarity). They act individually and together to regulate their own expression and that of numerous other sporulation-specific genes (By similarity). Binds promoters of target genes at brlA response elements (BREs) containing the conserved sequence 5'-(C/A)(A/G)AGGG(G/A)-3' (By similarity).
|
W6QY25
|
ANUC_PENRF
|
Oxidoreductase anuC (EC 1.-.-.-) (Annullatin D biosynthesis cluster protein C)
|
MSAPKGPITKFPAEGLRHARRFITTHNKEGKGVFAVDDDGDHHRIMVDGLAVANIIYSTSGNPVDMNDDNDLVYARDNEVRRFAGQINLFV
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Highly reducing polyketide synthase part of the gene cluster that mediates the biosynthesis of annullatin D, an alkylated aromatic polyketide with a fused dihydrobenzofuran lactone ring system that exhibits potent agonistic activities toward the cannabinoid receptors. The annullatin backbone 2-hydroxymethyl-3-pentylphenol is assembled from one acetyl-CoA starter unit and 5 malonyl-CoA elongation units by cooperation of the highly reducing polyketide synthase anuA, the short-chain dehydrogenase anuB and the oxidoreductase anuC, before being hydroxylated at the C-5 alkyl chain by the cytochrome P450 monooxygenase anuE to form (8S)-annullatin E. The prenyltransferase anuH subsequently installs one isoprenyl group at the benzene ring to form (8S)-annullatin J. Enzymatic or nonenzymatic dihydro-benzofuran ring formation between the prenyl and the phenolic hydroxyl groups in (8S)-annullatin J results in two diastereomers (2S,9S)-annullatin H and compound 12. The intermediate (2S,9S)-annullatin H is then converted to (2S,9S)-annullatin D by the FAD-linked oxidoreductase anuG-catalyzed five-member lactone ring formation. The isomer 12 acts as a substrate for the short-chain dehydrogenase anuF and is oxidized to (2R)-annullatin F, which is subsequently acetylated by an acetyltransferase leading to (2R)-annullatin G formation. The remaining enzymes identified within the cluster, anuD, anuI and anuJ, seem not to be involved in annullatin biosynthesis (Probable).
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W6R1D9
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AC891_PENRF
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Acyl-CoA ligase 891, peroxisomal (ACL891) (EC 6.2.1.-)
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MFFSQPTHLAKAEELKQAPPKGVAYSVALPGTEQPGRSPVYRAWNAQKELLTTLDPEVTTAHDIFESTAIRHPKNDCLGWRPYNSTTKSFDPYQWLTYETVQKRRAAFGAGIVELHHKHDCHRPGQYGVGLWSQNRPEWQITDLACVSQSLYSVSIYDVLSEDATEYIINHSELSCVVTSLPHIASLIKLKPSLPTLKIIISLDPLDGGEQAGHSKRAIFESMAAGLGLAIYTIDQVEELGLASKRGYNPPSASDIVTINYTSGTTGPPKGVVLTHGNAVAATSCGLITISQARGDTSASYLPLAHIYARLAEHTAFWGAARIGYFHGNIAELVDDLKLLKPTGFMSVPRLYSRFGSAIRAATVEQPGFKGALSRHIIAAKTANMKNPDPSKATVRHALYDRIWAKKVTAALGLERARYMVSGSAPLDPTLHNFLRVATGTDVLQGYGLTESYASATAQPVYDLTAGNCGSLAPCVEACLVSLPDMEYSVDDKPFPRGELLLRGNNMFREYYKNEEETRSAITEDGWFRTGDVCTIDEKGRFIIIDRRKNVLKLAQGEYISPERLEGVVLSELGYIAQAYVHGDSLQTFLVGIFGVAPDLFAPYASKVLGRTIAPTDLEAVKESLNDDKVRRAVLRDLERVAKKHKFAGYERIRNVSLKVEPFTVENNLLTPTLKLKRPPTVKVYRSLLDQLYEQAVEEQSAPKAKL
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Acyl-CoA ligase involved in the biosynthesis of mycophenolic acid (MPA), the first isolated antibiotic natural product in the world obtained from a culture of Penicillium brevicompactum in 1893 (By similarity). The peroxisomal acyl-CoA ligase 891 converts the intermediate MFDHMP-3C into MFDHMP-3C-CoA which impairs its diffusion from the peroxisome (By similarity). The first step of the pathway is the synthesis of 5-methylorsellinic acid (5MOA) by the cytosolic polyketide synthase mpaC. 5MOA is then converted to the phthalide compound 5,7-dihydroxy-4,6-dimethylphthalide (DHMP) by the endoplasmic reticulum-bound cytochrome P450 monooxygenase mpaDE. MpaDE first catalyzes hydroxylation of 5-MOA to 4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoic acid (DHMB). MpaDE then acts as a lactone synthase that catalyzes the ring closure to convert DHMB into DHMP. The next step is the prenylation of DHMP by the Golgi apparatus-associated prenyltransferase mpaA to yield farnesyl-DHMP (FDHMP). The ER-bound oxygenase mpaB then mediates the oxidative cleavage the C19-C20 double bond in FDHMP to yield FDHMP-3C via a mycophenolic aldehyde intermediate. The O-methyltransferase mpaG catalyzes the methylation of FDHMP-3C to yield MFDHMP-3C. After the cytosolic methylation of FDHMP-3C, MFDHMP-3C enters into peroxisomes probably via free diffusion due to its low molecular weight. Upon a peroxisomal CoA ligation reaction, catalyzed by a beta-oxidation component enzyme acyl-CoA ligase ACL891, MFDHMP-3C-CoA would then be restricted to peroxisomes for the following beta-oxidation pathway steps. The peroxisomal beta-oxidation machinery than converts MFDHMP-3C-CoA into MPA_CoA, via a beta-oxidation chain-shortening process. Finally mpaH acts as a peroxisomal acyl-CoA hydrolase with high substrate specificity toward MPA-CoA to release the final product MPA (By similarity).
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W6VBF4
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MDDA_PSESZ
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Methanethiol S-methyltransferase (EC 2.1.1.334)
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MNPPNRTGHRFFVFSGKLAGLLYSLCCYLFFLLTALYLIGFLAGIGVPKDINSGPGITWPLAVLVDAILITLFAAQHSGMARKNFKRWWMRFIPATLERATYVLSSCLVLALLFVLWQPIATPVWNVESPWGKGLLIALFWLGWGIVLLATFLISHFELFGVKQTLDAWRKRIPEKPAFKSPWLYKLVRHPLYVGFLIAFWATPDMTAGHLLFAILSTSYILIGAHLEEKDLVDSLGEVYQSYQQEVGMLVPKRNQTKGR
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Catalyzes the methylation of methanethiol (MeSH) to yield dimethylsulphide (DMS).
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W7DWT4
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VICT_BIPV3
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Probable transporter vicT (Victorin biosynthesis cluster protein T)
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MEKPTRQTPFYTQHRAELLVLSSQIAAALLHALARVVEVGSGLKERVHPFTVLQIRLFITVLGCTAYLWRARIDFLGPTGLRPLLALRAAGGVFGACGFYLSISYLSLSEATVLNFIAPLGAIMLTTYWEGRTFAFLDLIACITALAGVVLVLQPIPIYKAVAQAEISSSISTDPYAHLKGVVSGITGVAGGIVAFSAMNRLGKNVQPAVTINYFGVSICIVTTAFSTIMPEVVWPTRIESWCLLAIIGILGLVMEYLLTAGLGSDDPRVTIMIYSQVLWALFLDWAIWRSHVNVLTVLGSMVVVASLAVPYLFRESSHPKEDMFSTRSGMDDIEEGQDEAHANYISLE
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Probable transporter part of the gene cluster that mediates the biosynthesis of the secondary metabolite victorin, the molecular basis for Victoria blight of oats.
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W7DZP2
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VICYC_BIPV3
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UstYa family oxidase VicYc (EC 1.-.-.-) (Victorin biosynthesis cluster protein Yc)
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MLTKSRLQVFHELHCLNFLRKLIYPDVYGKIDYKGQIHANHCIDHIRRIAECGSNATPVVYTGYKNGNLYSEPETYTCRNFTLIRQWAEMKKIQNTQ
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UstYa family oxidase, part of the gene cluster that mediates the biosynthesis of the secondary metabolite victorin, the molecular basis for Victoria blight of oats. The role of vicYc within the pathway has still to be determined. The pathway starts with the processing of the precursor vicA1 by several endopeptidases including kexin proteases as well as the cluster-specific S28 family peptidases vicPa and vicPb to produce 7 identical copies of the hexapeptide Gly-Leu-Lys-Leu-Ala-Phe. After being excised from the precursor peptide, the core peptides are cyclized and modified post-translationally by enzymes encoded within the gene cluster. The ustYa family oxidase vicYb is required for the formation of the macrocycle in victorin and the copper amine oxidases (CAOs) vicK1 and vicK2 are responsible for converting victorin to the active form by oxidizing the N-terminal glycyl residue in the peptides to glyoxylate. Relaxed substrate specificity of enzymes in the victorin biosynthetic pathway results in a metabolic grid that produces a set of analogs including victorinines B, C, E or HV-toxin M (Probable).
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W7E3X3
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VICR_BIPV3
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Probable transcription factor vicR (Victorin biosynthesis cluster protein T)
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MSSPFQQILTTTSATNAIAASSAVPVECLHARGANSLASNAHTVLPGLDSQASPQSGQKEEMRRKNAEAQMQNDSNHSETTLFQSDLDTALQSLGYGSQTNQAYQNHPSRSREDITNSRAERHSQTSTQPKNVHAVSEPMATTSLDCGVLPLPSSALDEEFLNLDFPNQERIYIDLEPQHSNSTSSSSDEKCHCLSHIIQSLNRNRQGNHIRRDSMNKIHLLNEAAEQFLMCDSNHSKLWYIILLALYQDADDSLSSAEEPQERMGAHSGAKGFCGNIKSNLDTMVCHASLAWILNG
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Probable transcription factor part of the gene cluster that mediates the biosynthesis of the secondary metabolite victorin, the molecular basis for Victoria blight of oats. May play a role in the regulation of the production of victorin (Probable).
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W7E4C5
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VICYA_BIPV3
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UstYa family oxidase VicYa (EC 1.-.-.-) (Victorin biosynthesis cluster protein Ya)
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MDLYISNYTSDDDMAILRRRWIELLPLVVGDIVHVENPEGYSYLLDPIIPGPGYVVTWYHQLHCLFFLMSEYDRLLRHGPNGKERSIPAGSSSIHTRHCFEILRHSILCHLDMTLEGGSAPFFNGTTGFGHAHVCQNRQEAIDWMEKNRANDNRMIIRA
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UstYa family oxidase, part of the gene cluster that mediates the biosynthesis of the secondary metabolite victorin, the molecular basis for Victoria blight of oats. The role of vicYa within the pathway has still to be determined. The pathway starts with the processing of the precursor vicA1 by several endopeptidases including kexin proteases as well as the cluster-specific S28 family peptidases vicPa and vicPb to produce 7 identical copies of the hexapeptide Gly-Leu-Lys-Leu-Ala-Phe. After being excised from the precursor peptide, the core peptides are cyclized and modified post-translationally by enzymes encoded within the gene cluster. The ustYa family oxidase vicYb is required for the formation of the macrocycle in victorin and the copper amine oxidases (CAOs) vicK1 and vicK2 are responsible for converting victorin to the active form by oxidizing the N-terminal glycyl residue in the peptides to glyoxylate. Relaxed substrate specificity of enzymes in the victorin biosynthetic pathway results in a metabolic grid that produces a set of analogs including victorinines B, C, E or HV-toxin M (Probable).
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W7MC44
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FDB87_GIBM7
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NmrA-like family domain-containing oxidoreductase FVEG_08287 (EC 1.-.-.-) (Fusarium detoxification of benzoxazolinone cluster 1 protein FVEG_08287) (FDB1 cluster protein FVEG_08287)
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MSDNILVLGAGELGTAILEALAKHPSRANAKLSVLLRPSSINSTAPEKKKQIEHLQGLGITPQPGDVESSTSELAAIFRNYDTIISCNGMGRPFGTQTKLADAVFEAGVKRYFPWQFGMDYDAIGTGSDQDRFDEQINIRKKLRAQNKTEWTIVSTGLFMSFLFLTDFGVINLEQKVTRGLGTWDTKITVTVPRDIGRVTADIVFDPRGIANEVVHIAGDTLSYKEIADLVDERFGEGTFRRELWDMETLKKQLAEGRPVAEYKATFAVGKGVAWDREGTVNMARGIQMTGLREYLKDVNLVK
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NmrA-like family domain-containing oxidoreductase part of the Fusarium detoxification of benzoxazolinone cluster 1 (FDB1) involved in the degradation of benzoxazolinones produced by the host plant. Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively. The first step in the detoxification of benzoxazolinones involves the hydrolysis of the cyclic ester bond of benzoxazolinones by the FDB1 cluster gamma-lactamase MBL1 to aminophenols. MBL1 is able to convert BOA into 2-aminophenol (2-AP), as well as MBOA into 5-methoxy-2-aminophenol (2-AMP). The FDB2 cluster N-malonyltransferase FDB2/NAT1 then metabolizes aminophenols via N-malonylation to non-toxic malonamic acids. FDB2/NAT1 converts 2-AP into N-(2-hydroxyphenyl) malonamic acid (HPMA) and 2-AMP into N-(2-hydroxy-4-methoxyphenyl) malonamic acid (HMPMA). The duplicated dienlactone hydrolases DLH1 and DLH2 may provide redundant function for hydrolyzing the lactone moiety in the BOA molecule (Probable). The roles of the amidases an other enzymes encoded by the 2 FDB clusters have not been identified so far (Probable).
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W7MLD3
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FUS6_GIBM7
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Efflux pump FUS6 (Fusarin biosynthesis protein 6)
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MPQPDKMAAVNNAMPQPAPEKSLSSDPQPESSKKSARFWLIFVAIALTTFLAALDTSIISTALPTITADLGSESLYVWIIDAYLLASTATIPIFAQAANIYGRRSLTLIAVCIFTLGSGLCGGAHNTAMMVGGRAVQGIGGGGILTMSEIVVCDMVSIRERGMYAGIIGGVWAIAAVVAPVMGGAFAQNISWRWIFYINLPIAGVSLVALGLFLKLARPPSGTVKEQMSRIDWGGSVLLIGSVTSIVLALSWGGSEHPWSGWQTIVPLVIGLLALVAFFAYQGAPWLREPTMPLRLFGNRTSSTLLVISFIHSLLLYWVCYFLPVYFQAVKEASPTRSAVMLFPIACTSAPAGVAAGITITKTGKYRVWHFTGFVLMSIACGLFTLLDAQSSTGRWVGFQILFGVGTGTVFTSTLPPILASLPDSDVATATGAWTFIRNFGSIWGVAIPAAVFNNQVNHAAPKISDSTVKSLLVDGGAYEHATQHFIKSLSPNPELKTQVIQVYLEGLKVVWQVSLAFCLLGFILCFFVRSLTLRDELNTEFGLKEEKPNSKNMSSEEGVVRE
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Efflux pump part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production (By similarity). The other FUS cluster members are not essential for fusarin C biosynthesis (By similarity).
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W7MMJ0
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FUS3_GIBM7
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Glutathione S-transferase-like protein FUS3 (EC 2.5.1.-) (Fusarin biosynthesis protein 3)
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MTSFGTLYTYMPNARVFKILAAAKLNNLIIEIPAYQHGVTNKSAEFLSKFPAGKVPAFEGPDGFCLVESDAIAQYVAQSGPQASQLLGQDAMSSAKIRQWISFFAEEIYPTVLDLVMWRVGLGAFDETTEIKALAQLAYGLSVLEKHLNPGILLTGDELTLADLTGASTLLWAFMHIIDEPMRQQYPNVVAWYLKVVQNEEVKEVFGKPNLIEKRRIGAK
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Glutathione S-transferase-like protein part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production (By similarity). The other FUS cluster members are not essential for fusarin C biosynthesis (By similarity).
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W7MPI5
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WOR1_GIBM7
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Global transcription regulator sge1
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MSGTTQLRPTYHGYVRDTTDALIIFEACLAGQLLHVPRRPHDRERQNVIKSGSIFVYEEHASGIKRWTDSITWSPSRIMGNYLVYRQLEKPFAPGEKKRAKGKGGKSTTQSGGISKPRQRNALPFQQGLEQGNEYPSVPSDEDRQLVGSLVDSYDFKEQGLVKKTISITYNGVPHHLISYYTVEDVKAGLLTSPADDQGLRGVVPRAELTNGQNFRAPIEESIGGAYMPGMRHSAGFPHPSAYPTLLHQPQMHQPQVHQPLAHQPQVHQPLAHQPQVHQPLAHQPQVHQQYVHQPQAHQPYMHQPQVHLNGYQPSYGDGQWWKYLGGT
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Global transcriptional regulator of transcription that impacts, but is not absolutely required for secondary metabolism and pathogenicity on maize. Regulates synthesis of multiple secondary metabolites, including fumonisins and fusarins.
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W7MTI3
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FDB26_GIBM7
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MFS-type transporter FVEG_12626 (Fusarium detoxification of benzoxazolinone cluster 2 protein FVEG_12626) (FDB2 cluster protein FVEG_12626)
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MDPDTEQMRVEKPNHEQPKPNTEFPDGGFKAWSVVVGAFCGLFVGVFQAYYEANQLQDLSPSTVSWIPAISMFIMFITGPFVGRAFDNYGPRYLLLAGTLLHVFGLMMASISSQYYQYILSQAICSPLGAAMVLYPSFSCVTTWFRQKRALALGITASGSSLGGTILPIVVNRLIPRIGFGWTMRACAFLLLGLLLVTNLTVRSRVAPQPKEAGIIAYLRPFTSLSFILTSLAGFFYSMGMFIPITFMVTYGEHVGLSNSMAGYLVSIFNASSGIGRILPGYIADKVGSFNVSIAAATLSTIFMLGLWLPGHSRESAIAFAALFGFSSGTYTAISPALIAHISDLEEIGTRSGTMYAFMSVAALTGSPIGGALISSAGGSYWKLQVFAGCMLGAGTVFYVLARLYITKGRLWEKV
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MFS-type transporter part of the Fusarium detoxification of benzoxazolinone cluster 2 (FDB2) involved in the degradation of benzoxazolinones produced by the host plant. Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively.
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W7MVT8
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FDB94_GIBM7
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Transcription factor FVEG_08294 (Fusarium detoxification of benzoxazolinone cluster 1 protein FVEG_08294) (FDB1 cluster protein FVEG_08294)
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MAPPSVENGSDTSTAKRRRIALACNACRLRKSRCDGTRPSCSSCVSLTLDCQYEPGESAANVIVRKQYISDLESRVYNVEQVVHRLNYFFEGHLSACATATGNATVTAAAAQSRLPRIPSPPAPSSSALEETNDGSHPHATGLEEPQDEDATTNGMAMTFVEEHTSAFFGGSSNINFTRLLLKAVNNIRNPARRLGATVDQQHELSETNLAKASRSYTNPVAASPDTGPKAMTTLPPAQEMDRMLDVYFKTAGTVFPFIHEESMRKTYTTCKASNWTRVRRTFLGTLNVIFATIASADQDAIPSARERQERSNIFFKRATALCSELSKQVISIEIVQYLVLVVIHCQGAQRSVQAWNILGLAVRSAMALGLHSAQAREGLDELQAEYSRRTWVVIYCMDKVLSVAFGRPAIIPDEYMLDQPSSSSEVAMPTPDSAGTGVDIPGDFLAVSFRLHQIMNGSLRQQYGGNVHTAEPEPDDMMSLQASGQLRKELRAWSASLPPYLRLCEPKAKIPSENTSVNRLRVILTLRYHNINMLIHRPLLCSTIRHLFLGGNSVSIDNSSYIIQLAMGEAHESLRSAQHTIELVHTIIKADPSGSNNLGVAYFTLHYVFTASLVVLGRILWAQHGQGAAADETALAMCKSLLGQVETIFQLLDHDNSLVYSCSRYINNMLEVCTAQDAIVAVQNAESGDSSAHQPPSSLAAKQLETMMHLGMGDMEMFQAYSSQIYDPALSEGLDTSSVEAATARNTDWENSFWAM
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Transcription factor part of the Fusarium detoxification of benzoxazolinone cluster 1 (FDB1) involved in the degradation of benzoxazolinones produced by the host plant. Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively. Might be involved in the regulation of the expression of the FDB1 cluster genes (Probable).
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W7MWX7
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FUS5_GIBM7
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Esterase FUS5 (EC 3.1.2.-) (Fusarin biosynthesis protein 5)
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MVHRPRLLCLHGGGASSQIMRIQFSKLESALRKTFQLVFLEGPLDSAPGPGVLPFFKDFGPYSCWVSDDRSLSPEEKRQEETNAIAYIKTFMLQYGPFAGILGFSQGARAAASILLEQQREAFTHDSLFGVFFCGTFPPFIPDAPDISLPTIHVLGLTDPYLRESEVLLEHCTQQSVRRVIKFNGGHHMPTSSDVTQQIADVISMTYRTSQRKRVSGIWKKNVVDSRPSALEI
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Esterase part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production (By similarity). The other FUS cluster members are not essential for fusarin C biosynthesis (By similarity).
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W7N2B2
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FUB2_GIBM7
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Fusaric acid biosynthesis protein 2
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MASELKEYLVIIPDLPDVLAKRQVLLKPHNQDAAPLVKAGRVPFFGSTLAHHSAEGQQVAENGTVMIIKAESEEEIKEIIRKDIFTIEGVWDFGRLSIWPFKSK
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Part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties. L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L-homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O-acetyltransferase FUB5, as well as enzymes of the primary metabolism (By similarity). The polyketide synthase (PKS) FUB1 generates the triketide trans-2-hexenal which is presumptively released by the hydrolase FUB4 and linked to the NRPS-bound amino acid precursor by NAD(P)-dependent dehydrogenase FUB6 (By similarity). FUB1, FUB4, and the non-canonical NRPS Fub8 may form an enzyme complex (By similarity). Further processing of the NRPS-bound intermediate might be carried out by FUB6 and the sulfhydrylase FUB7, enabling a spontaneous electrocyclization to close the carbon backbone of fusaric acid (By similarity). Dihydrofusaric acid is likely to be released via reduction by the thioester reductase (TR) domain of FUB8 whereupon the final oxidation to fusaric acid may (also) be performed by the FMN-dependent dehydrogenase FUB9 (By similarity).
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W7N2P0
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DLH2_GIBM7
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Dienlactone hydrolase 2 (EC 3.1.1.-) (Fusarium detoxification of benzoxazolinone cluster 2 protein DLH2) (FDB2 cluster protein DLH2)
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MDNVLARPADICCLKGSFHSGDATGSTIQIDGIDTYVAKPHPDKSNGNVLLFFPDAFGLHINSFLMMDAFAECGYLTLGVDYFLGDPVTKHSLTPLSDPNFDFESWKNKHLKASEDAAARWVKAVKAQYGSSEDVRFACVGYCWGARFVCQQLSADAPIFFSVPSTDKLFEPEQRSRTIEILTENNKQFNMQVFANVGHGFASRARLTDPYEKWAKEATFKSFVDWFDFWMEKK
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Dienlactone hydrolase part of the Fusarium detoxification of benzoxazolinone cluster 2 (FDB2) involved in the degradation of benzoxazolinones produced by the host plant. Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively. The first step in the detoxification of benzoxazolinones involves the hydrolysis of the cyclic ester bond of benzoxazolinones by the FDB1 cluster gamma-lactamase MBL1 to aminophenols. MBL1 is able to convert BOA into 2-aminophenol (2-AP), as well as MBOA into 5-methoxy-2-aminophenol (2-AMP). The FDB2 cluster N-malonyltransferase FDB2/NAT1 then metabolizes aminophenols via N-malonylation to non-toxic malonamic acids. FDB2/NAT1 converts 2-AP into N-(2-hydroxyphenyl) malonamic acid (HPMA) and 2-AMP into N-(2-hydroxy-4-methoxyphenyl) malonamic acid (HMPMA). The duplicated dienlactone hydrolases DLH1 and DLH2 may provide redundant function for hydrolyzing the lactone moiety in the BOA molecule (Probable). The roles of the amidases and other enzymes encoded by the 2 FDB clusters have not been identified so far (Probable).
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W7N463
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FDB29_GIBM7
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Acyl-CoA transferase FVEG_12629 (EC 2.8.3.-) (Fusarium detoxification of benzoxazolinone cluster 2 protein FVEG_12629) (FDB2 cluster protein FVEG_12629)
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MTTKTSNETYGAGTVVDSEFSPLPAECERILRIFAARTPGFTKDEALLSGVNFHGDDLPCIPGPIKSQAVTAVLHAMVGIVGLEILHLRGVTTDNQIDIDVNHAGLYPATAALVDIDGVTGPEVIKLPTVPQWDKDRASNSPLVYRATAIYETADSGVWFQLHGSLDSWKVLALLGIGKDLDSEIRTNDAAYELIQERVRKYRAREIEQLVVEKGLSGSIVYSPEEWRQTEMGRSLSRHPLVNYKQKSHCATLAPASFPVLEDKRPLAGIKVVELTRIIAGAAAGAALASLGAEVIRVNSSKLKDYTPAQPSSLMAGKKTIDLDLEDPADHKKLMQLFEQADVILQGYRLGSLARRGFGLEAALELANKRGRGVVYVDENCYGPDGYYAERPGWQQVADAAAGSSYVMGQSFGFPKGQGVLPSLPISDMSTGILTALTIMCGIRDRAKFGGSYHGHASLTAYNMATLDSEVRLYQREVVQKISDKYEFPTWSSDVHVAPLYYSILDAWGKKSELIKDEKHYIHFSDSVFGSDLRVLGPVVRYDKEEYSPKWNSPPVPFCHHEFTMFSNQ
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Acyl-CoA transferase part of the Fusarium detoxification of benzoxazolinone cluster 2 (FDB2) involved in the degradation of benzoxazolinones produced by the host plant. Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively. The first step in the detoxification of benzoxazolinones involves the hydrolysis of the cyclic ester bond of benzoxazolinones by the FDB1 cluster gamma-lactamase MBL1 to aminophenols. MBL1 is able to convert BOA into 2-aminophenol (2-AP), as well as MBOA into 5-methoxy-2-aminophenol (2-AMP). The FDB2 cluster N-malonyltransferase FDB2/NAT1 then metabolizes aminophenols via N-malonylation to non-toxic malonamic acids. FDB2/NAT1 converts 2-AP into N-(2-hydroxyphenyl) malonamic acid (HPMA) and 2-AMP into N-(2-hydroxy-4-methoxyphenyl) malonamic acid (HMPMA). The duplicated dienlactone hydrolases DLH1 and DLH2 may provide redundant function for hydrolyzing the lactone moiety in the BOA molecule (Probable). The roles of the amidases an other enzymes encoded by the 2 FDB clusters have not been identified so far (Probable).
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W7N6M8
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FUS9_GIBM7
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Methyltransferase FUS9 (EC 2.1.1.-) (Fusarin biosynthesis protein 9)
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MADKSHVNNVPMQGNGAYSSHAALQHEAMLKALPLFRAAAEAISKVDSTRVAIVEYGSAHGNNSLEPMEAILKSIHARSLELLFSDRPENDFCTLSKTVTEWADGLVENQLLHPLFISMIPRSFYQQVIPPKSAHLGFSLAALHHLDHVPQPTEDGQDESKLLQRQAHVDLATFLKLRSKEIVSGGSLILSFVGQASAGYENYGGPVDACRNAMIQMVQQDKIPVSVAQAFRVPTYNRTLSDVKKLMDEFTQIWKVHDLFEDDVMHPAFYELKIQSNPSQEASHKYAEIVIDWMMAVCSGYFTKALQVGSQGGYTKEEEESLLQDWVTRTKELFIRDHKDEEVICSFIYIRLERL
|
Methyltransferase part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production (By similarity). The roles of the other FUS members are yet undetermined (By similarity). The fusarin C synthetase FUS1 is responsible for the condensation of one acetyl-coenzyme A (CoA) unit with six malonyl-CoA units and the amide linkage of the arising heptaketide and homoserine, subsequently releasing the first intermediate, prefusarin, as an alcohol with an open ring structure. The cytochrome P450 monooxygenase FUS8 participates in multiple oxidation processes at carbon C-20 and is able to use the FUS1 product as substrate, resulting in formation of 20-hydroxy-prefusarin (By similarity). This reaction seems to be essential before the 2-pyrrolidone ring closure can be catalyzed by FUS2, generating 20-hydroxy-fusarin (By similarity). FUS8 is able to further oxidizes carbon C-20 after ring closure, resulting in the formation of carboxy-fusarin C (By similarity). As the last step, FUS9 methylates the hydroxyl group at C-21 to generate fusarin C (By similarity). Fusarin C can then rearrange to epi-fusarin C, the (z)-isomers, and fusarin A and fusarin D (By similarity).
|
W7N6P0
|
FUS2_GIBM7
|
20-hydroxy-prefusarin hydrolase FUS2 (EC 3.7.1.-) (Fusarin biosynthesis protein 2)
|
MHKVFASDFFNFEFLRLLGTVPFQGAEVGECLTTAGRIKDGDPESWYRAWRDQAEKAQALAEEAAAVGDRTGACWAYIRAANYWRASEFLLHCTPNDPRILAASKASVNAFDKGWVLLDATVKSFEIPYDKDIKLPGRLYLPAPHHRLPGKIPVVLQTGGFDSTQEELYFYGAAGALPRGYAVFSFDGPGQGLPLRVGKLKLRTDWEYVVSQVLDFVTDDIAPEYDLDLERLAIFGASLGGYLSLRAAVDPRIKACISCDGPLDLFEITRSRMPSWFINGWLSGWVSDGLFNWVVDALTAVNFQIAWEFGHGKWVFGVETPADVLRVMQQISLKGGYLSKIKCPTLITGAADSFYFTPDINANPIFEGLTALGSNEKHLWIGKGVEGGGLQAKIGALAVVHHKMFTWLDSTFAIKRDVL
|
20-hydroxy-prefusarin hydrolase part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production (By similarity). The roles of the other FUS members are yet undetermined (By similarity). The fusarin C synthetase FUS1 is responsible for the condensation of one acetyl-coenzyme A (CoA) unit with six malonyl-CoA units and the amide linkage of the arising heptaketide and homoserine, subsequently releasing the first intermediate, prefusarin, as an alcohol with an open ring structure. The cytochrome P450 monooxygenase FUS8 participates in multiple oxidation processes at carbon C-20 and is able to use the FUS1 product as substrate, resulting in formation of 20-hydroxy-prefusarin (By similarity). This reaction seems to be essential before the 2-pyrrolidone ring closure can be catalyzed by FUS2, generating 20-hydroxy-fusarin (By similarity). FUS8 is able to further oxidizes carbon C-20 after ring closure, resulting in the formation of carboxy-fusarin C (By similarity). As the last step, FUS9 methylates the hydroxyl group at C-21 to generate fusarin C (By similarity). Fusarin C can then rearrange to epi-fusarin C, the (z)-isomers, and fusarin A and fusarin D (By similarity).
|
W7NCN7
|
FUB6_GIBM7
|
Dehydrogenase FUB6 (EC 1.-.-.-) (Fusaric acid biosynthesis protein 6)
|
MGGEVSNKTWVFKKSPSSLPEPGVHTAFEDRPLSLVAPPGGLVIKLLTAGLDPHQRDRMRGAGNVDYVPGYELDEPITNFSIAKVIRSDNDAFEEGSLIAGSLPIAEYGIIPKELIDARAMASPLVWKVSNNYNLDLKHYVGTLGLAGMTAWNSFYGLVKPVKGETIWINAASSSVGEVVVQLAKIEGMKVIASVSSDEKLDYVVNELGADVGFNYQKEPVGKALKRLAPDGLDVVFENVGGDHFQAAIENMKWFGRIISCGTASQYNKPVEEQYGVTNLSEIFRRRIKIQGFIFWDDNIYTDNIENFKATMPKWVSEGKIKSRYTQFEGIEQADKAFLSMFTGGSHGKTVLKISDP
|
Dehydrogenase part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties. L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L-homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O-acetyltransferase FUB5, as well as enzymes of the primary metabolism (By similarity). The polyketide synthase (PKS) FUB1 generates the triketide trans-2-hexenal which is presumptively released by the hydrolase FUB4 and linked to the NRPS-bound amino acid precursor by NAD(P)-dependent dehydrogenase FUB6 (By similarity). FUB1, FUB4, and the non-canonical NRPS Fub8 may form an enzyme complex (By similarity). Further processing of the NRPS-bound intermediate might be carried out by FUB6 and the O-acetylhomoserine FUB7, enabling a spontaneous electrocyclization to close the carbon backbone of fusaric acid (By similarity). Dihydrofusaric acid is likely to be released via reduction by the thioester reductase (TR) domain of FUB8 whereupon the final oxidation to fusaric acid may (also) be performed by the FMN-dependent dehydrogenase FUB9 (By similarity).
|
W7NDQ0
|
FDB40_GIBM7
|
Transmembrane transporter FVEG_12640 (Fusarium detoxification of benzoxazolinone cluster 2 protein FVEG_12640) (FDB2 cluster protein FVEG_12640)
|
MASPTISSMEQYTPSSKDEKIVPLHGDAAGSDTEKGESREVFQENVDGVEFRTVSWQRATVVFLKINFAMSILAIPGALGALGSVGGSLCIVGYTSLNVYTALVLGDFKHNHTECHTLADMMGLIWGRWGRELVGVQIIVAQVLISAGGIVTSAIGLNALSDHGTCTVMFALVSAILITLFSSIRTFARLGWLTWFGFITFVLGVFIFVVAVTQVDRPAAAPKTGDFELGWAPIAYPSFVVGMINATNIFISTCGSSMFLPVISEMKRPHDYRKACLVAGFIVGAMYLSFSLVIYRWCGTWISTPAFGSAGPLIKKVAYGVSLPGLILGVGIYQHVAAKYAFVRILRDSEHLQANTFTHWGTWLGINLALGTAAFIVAEAVPILNYLLGLAGSLCFAPFSLVFPALLWMYDFKSYKTGTLGQKIKYGLHILIMILGFYMIVAGTYSVAVLIKEAFNTGAIAKVFDCADNSGFVQ
|
Transmembrane transporter part of the Fusarium detoxification of benzoxazolinone cluster 2 (FDB2) involved in the degradation of benzoxazolinones produced by the host plant. Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively. Might be involved in the transport of metabolites of benzoxazolinone degradation (Probable).
|
W8P570
|
PRF03_KALTU
|
Profilin Sal k 4.0301 (Allergen Sal k 4.03) (allergen Sal k 4.0301)
|
MSWQAYVDDHLMCEIEGTNNHLTAAAILGVDGSVWAQSANFPQFKPDEISAVVKEFDEAGTLAPTGLHLGGTKYMVIQSEAGQVIRGKKGPGGICVKKTGQALIFGIYDEPVTPGQCNMIVERLGDYLIEQGL
|
Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations.
|
X5IFY8
|
COW_CONGE
|
Contryphan-G
|
MGKLTILVLVAAVLLSTQAMVQGDGDQPAARNAVPRDDNPDGPSAKFMNVQRRSGCPWEPWCG
|
Its target is unknown, but this toxin may modulate voltage-activated calcium channels (Cav) or calcium-dependent potassium channels (KCa).
|
X5IFZ1
|
CAI19_CONGE
|
Conotoxin G1.9
|
MGMRMMFTVFLLVVLATTVVSFTSRRGPKSRRGEPVPTTVINYGECCKDPSCWVKVKDFQCPGASPPN
|
Does not show activity on all the human nAChR subtypes studied.
|
X5IXY8
|
CSST2_CONGE
|
Consomatin G2 (ConSST G2) (Somatostatin-related peptide) (SSRP)
|
MQTAYWVMLMMMVCITAPLPEGGKPNSGIRGLVPNDLTPQHTLRSLISRRQTDVLLDATLLTTPAPEQRLFCFWKSCTWRPYPWRRRDLNGKR
|
Moderately activates human somatostatin receptors (SSTR) with a preferential activation of SSTR1 and SSTR4. In vivo, does not cause behavioral changes in mice within a few minutes of intracranial injection, but causes a progressive loss of movement thereafter. Four to five hours after injection, mice recover, even with the highest dose tested. Shows antinociception and antihyperalgesia activities in two mouse models of acute pain, most probably by acting outside the central nervous system.
|
A0A068Q6B2
|
ANCHR_BPKNT
|
Anchor protein (Gene product 28) (gp28)
|
MAFSWQEQIKPAGTQDIQCDIEYLDKSYIHVYLDGAETTGYTWTSATNIRLNTALAASTTVLLIRKTEREYLYIEFASGSPFIEVNVDSQNTQFLHLAQELVEGRAIPGFYGTISMNGYRITDLANPINAQDAATKAYVDTADTLLGQRIDAEHSGWVSAVHAEAVTRKAADDALSMRTSALENTFISGVETVSYPWSAVLTAATDEVTPGLAFTKAVVEINGVGQIRGYSFEIVDNTILFAEVLPAGTVVAARLGADVTAGDGFATQASVDYLANSLGDLAYLDKAAAVSDATSTGDVVAKLNALLAALRTSGVLAT
|
Anchors indirectly the receptor binding (RBP) protein (depolymerase) to the virion.
|
A0A084API5
|
SAT15_STACB
|
Satratoxin biosynthesis SC2 cluster transcription factor SAT15 (Satratoxin biosynthesis SC2 cluster protein 15)
|
MTTPPGWKVSGQNEISRPFDILEAWFHRIVGGGNLTRERDSFGSNYVVKLGFPGSVADPIPYLRRAWLVTRYLHPQLGATYSSKSLDDLRYIIRPLDEQIWLQTTFFVEQGPSATYSSAEDAVSKYLSKSTTTAHWIPATSEFMISPTASSPL
|
Transcriptional regulator that may regulate the expression of the satratoxin biosynthesis SC2 cluster, one of the 3 clusters involved in the biosynthesis of satratoxins, trichothecene mycotoxins that are associated with human food poisonings.
|
A0A084B9Z7
|
SAT9_STACB
|
Satratoxin biosynthesis SC1 cluster transcription factor SAT9 (Satratoxin biosynthesis SC1 cluster protein 9)
|
MASAALFYDSRATIARRLTLHCQYMARAVLFAQCRSAETMLTFILDLSWLFPDENGMRDNTCCYIVATITMALDLLRDRVLAVAVSLDVELLPYVYIVVTHTRLHLLASLLNYPPVHLDVRRMVSEAALHSACEVLRAAVRGEDQLKYIPNNLVIMICYASCISHVPKVRRLVAQLLQFSWTKQGLFTHCVSLLVATLAAKSGSQNSR
|
Transcriptional regulator that may regulate the expression of the satratoxin biosynthesis SC1 cluster, one of the 3 clusters involved in the biosynthesis of satratoxins, trichothecene mycotoxins that are associated with human food poisonings.
|
A0A098D1N7
|
GRA6_GIBZE
|
Gramillins biosynthetic cluster protein FGSG_00038
|
MSNIAHGNPQKRPGYAIDIEASCRKRGKSAPAEDCLNEAKTPLDEIESRVVALQRQIANLNSGTLLQSIKEATARLATSWALVTKHQRYVDGYQELALPDAPTYHVQALKTAQSDLEKASQDAQAADGVLASAQKEQRDFKRVEENLVMLGAERATLDQSVRDLTLDKERCDVYLGMVEYGPDGLATLLEKDVGAWKGMLDLV
|
Part of the gene cluster that mediates the biosynthesis of gramillins A and B, bicyclic lipopeptides that induce cell death in maize leaves but not in wheat leaves. The nonribosomal peptide synthetase GRA1 incorporates respectively a glutamic adic (Glu), a leucine (Leu), a serine (Ser), a hydroxyglutamine (HOGln), a 2-amino decanoic acid, and 2 cysteins (CysB and CysA) (Probable). The biosynthesis of 2-amino decanoic acid incorporated in gramillins could be initiated by a fatty acid synthase composed of the alpha and beta subunits FGSG_00036 and FGSG_11656 (Probable). The cytochrome P450 monooxygenase FGSG_15680 could hydroxylate the fatty acid chain (Probable). Subsequent oxidation to the ketone by the oxidoreductase FGSG_00048 and transamination by aminotransferase FGSG_00049 could form 2-amino-decanoic acid (Probable). On the other hand, FGSG_15680 could also be responsible for the HO-modified glutamine at the gamma-position (Probable). Whether hydroxylation occurs on the fully assembled product or on the Gln residue prior to assembly into the gramillins requires further proof (Probable). The thioredoxin FGSG_00043 could also be required for the disulfide-bond formation between CysA and CysB (Probable). The specific involvement of the remaining proteins from the cluster is more difficult to discern, but could have broader regulatory (FGSG_00040 and FGSG_11657) or enzymatic functions (FGSG_00044 and FGSG_00045) (Probable). The final C-domain of GRA1 does not possess the expected sequence of a termination CT domain, often implicated in macrocyclization and release of a cyclopeptidein fungal NRPs and the thioesterase FGSG_00047 may act in concert with the terminal C-domain of GRA1 to catalyze the formation of the macrocyclic anhydride and release of the products (Probable).
|
A0A0A8J8T2
|
DPO24_BPK64
|
Depolymerase, capsule K1-specific (Probable tail fiber protein)
|
METEGLTLDWNAHLPTVEVAYGLTKNSLKMWKSGTTATSDDYWLYTDGTVWNGVGVLGNNPETSTGFEKITPNFNASIKTYSASATDGQTDFNIPFTFSTITVFVNGSIQLPGLNYTVSGSTLTFTTELEAGDLLYVFIGNPNISTNDKLNRIYTANAMQGQTTIQVPYDFSTAIVYINGVLQNPITAYSIGADRIITFSEELYQDDEIIIMLGDIIIQSDEYVLKQELLDVNASSYINTKSGNSIQEEFDILYNSNSISKIIYSDIKNINWDEINEIFVCGKTLNTTEGAGYFYYDNNDTITVEDGGTCFVINNKRIKRRYIGPALSSWFTTIDGINTFLSTGNVSLRFDSNLTLTKALTIKSNTNLYFNKDVFLFPSGPTIQGLICSGSVSTTITTTLTSDVSSSSFIVNVTDASKFSVGDYVEIRSEKLVEGVNAQGVKIGIMRQITKIDANQLYIDKIALYDFTISDNTLISKMDIVKNVNIDGLTFNNINYTTLFPITMNMVYCDNIVIKNTQLYGSKEKYTGDVSGRTALKINSCRNVLIENCNAYHQGWYGVEILGYSEEVTVDKCFFDDCRHGVSINWSSIYGEPNGILINDCTSTSSTLSGFDTHDIGRNITFSNCRAYKSGDDGFQIRARNVKYINCLADYSTLDGFGQGDGAINTRLIGCKATNNGRNGFSLVWEGGNIEDCEALNNQYGYAMLGGRIINSRGIDNSSACVDCGSNSDPANQFSLYIDNCDFPYSTIQTRCLYFRGSSGIRPELVSVKNTNMAGYGNLWYLLGGYSSQPLSPMLNNNTLDINSTTAPTSGMVTLTAGTATINTSAVKLSTSSTASTLRYVSNIDLKRILSSSNIGTLSISNIVNGVSFTITSSNNLDASTIYWQISL
|
Functions as a receptor binding protein (RBP) and probably mediates the attachment to the host capsular exopolysaccharides (Probable). Displays a lyase activity that specifically degrades the K1-type polysaccharides of Klebsiella pneumoniae capsule (Probable).
|
A0A0H2ZKA1
|
TIS1_PSEAB
|
Immune protein Tis1
|
MAIEKGEAFARRDIYIDYDFEDVTYRWDHRQGTIHVRFYGEAESPEPVEHDNRLFNDALRFGREITREEYETGFPKG
|
Immunity protein that plays a role in preventing early activation of toxin Tas1.
|
A0A0H3MAZ5
|
IFTNT_MYCBP
|
Immunity factor for TNT homolog (IFT homolog) (Tuberculosis necrotizing toxin homolog antitoxin) (TNT homolog antitoxin)
|
MTIGVDLSTDLQDWIRLSGMNMIQGSETNDGRTILWNKGGEVRYFIDRLAGWYVITSSDRMSREGYEFAAASMSVIEKYLYGYFGGSVRSERELPAIRAPFQPEELMPEYSIGTMTFAGRQRDTLIDSSGTVVAITAADRLVELSHYLDVSVNVIKDSFLDSEGKPLFTLWKDYKG
|
Antitoxin for tuberculosis necrotizing toxin (TNT) homolog. Acts by binding directly to TNT, which inhibits NAD(+) glycohydrolase activity of TNT and protects M.bovis from self-poisoning.
|
A0A1P8YT88
|
CAPSD_AHEBV
|
Capsid protein
|
MFTALEKVVDTLRLRIFCFSACCNEVNASKKKGKKMSANEIKNQLHVMHDPFSDKTSQPKIPDGKANESLGFATQTVQEVGNAEGANTMHILLFPGQNSGILIDETAQADLGSRTYYIPTFFGSNGLDWDDLADATTAANVRGLDNYALWRVVSTGLQLKLLNPVDQDDGWWESVRVTTENTNVDWYLTTGNNSTQPGGNNGTIAPVGLINSLLSQQTLANEQSYSTGLLRDLHRVQFECHGQRDYHDFIQQRNEIRLAGAAISAVDKTTNYEAQFSLGHDDANDVINQFVDRSYDMVYIRLHCRQNTGTTPFLGSRFHLNCVSNQEVIFDHEERESRFHTRSHTIGSNANSVHMQARRADQNAAKMTM
|
Self-assembles to form the virion icosahedral capsid.
|
A0A1P8YT89
|
REP_AHEBV
|
Replication-associated protein (Rep)
|
MFLAAIHVITFFISENSKSFYTMSTPTSAFNAMLDDIGIEIQDDISALCSTLADPSDAEPAPPVHDVDDLLASVGPDKRKKIRSGLLTIHPPSSHPSWLKPETWFPQCDDILEIWCAKFEKGEDTGNLHVHIYFKLKHSNTIRFELLQKWITKHVTGFDFKPQRSATKNSTQCVVNYVLKPETSVGDPFIWNASCAFDQKTWDARHKGKGKKQEIIDHIMARDWTLSWASLVHESDESRALLADCGWGKRFQEDRAAAQPRRKIKDVVILYGAAGTGKTTMAMDWDSKPDETTKARYYRRSCDEDFWGGGATAYNGQRVIHYDEFGGQEKFASLKEITSIGLPGPPVKVKGSGRDLNHDTVVFTSNVHPAGWYKGVWAKDPHQFKPFQRRVTKVLFFPRERPDGTENVPSDGNPAHFVDQTPEWVAFGDNLDLAIEHAESCWPLPATIEDDGGGAFAPGFSLTSEPEPKRRRFF
|
Plays an essential for the replication of viral DNA. Presumably cleaves viral genomic dsRNA replicative form to initiate rolling circle replication.
|
A0A7H0DN28
|
PG055_MONPV
|
Protein OPG055 (Protein F11)
|
MGFCIPLRSKMLKRVSRKSSSILARRPTPKKMNIVTDSENRLKKNSYIENTNQGNILMDSIFVSTMPVETLFGSYITDDNDDYELKDLLNVTYNIKPVIVPDIKLDSVLDRDGNFRPADCFLVKLKHSDGFTKGALYLGHSAGFTATICLKNEGVSGLYIPGTSVVRSNICQGDTIVSRSSRGVQFLPQIGGEAIFLIVSLCPTKKLVETGFVIPEISSNDNAKIAARILSEKRKDIIAHINTLIQYRQQLELAYYNSCMLTEFLHYCNSYADTIKESLLKETIQKDINIIHTNITTLLNETAKVIKLVKSLVDKEDTDIVNNFITKEIKNCGGVKNRDKIVNSLSLSNLDFRL
|
Stimulates increases in peripheral microtubule dynamics and may increase the motility of the infected cells, contributing to cell-to-cell spread of the virus. Seems to inhibit the signaling via the GTPase RHOA and DIAPH1/mDia.
|
A0A7H0DN40
|
PG067_MONPV
|
Protein OPG067
|
MINDDSFTLKRKYQIDSAESTMKMDKTMTKFQNRVKMVKEINQTIRAAQTHYETLKLGYIKFKGMIRTTTLEDIAPSIPNNQKTYKLFSDISVIGKASQNPSKMIYARCFTCFPICLEMTIDSFVIECIQHCS
|
Major early protein present in virus factories. The presence of BEN domains suggests a possible role in organization of viral DNA during replication or transcription.
|
A0A7H0DNC0
|
PG148_MONPV
|
DNA polymerase processivity factor component OPG148
|
MTSSADLTNLKELLSLYKSLRFSDSVAIEKYNSLVEWGTSTYWKIGVQKVTNVETSISDYYDEVKNKPFNIDPGYYIFLPVYFGSVFIYSKGKNMVELGSGNSFQIPDEIRSACNKVLDSDNGIDFLRFVLLNNRWIMEDAISKYQSPVNIFKLASEYGLNIPNYLEIEIEEDTLFDDELYSIMERSFDDTFPKISISYIKLGELKRQVVDFFKFSFMYIESIKVDRIGDNIFIPSVITKSGKKILVKDVDHLIRSKVREHTFVKVKKKNTFSILYDYDGNGTETRGEVIKRIIDTIGRDYYVNGKYFSKVGIAGLKQLTNKLDINECATVDELVDEINKSGTVKRKIKNQSVFDLSRECLGYPEADFITLVNNMRFKIENCKVVNFNIENTNCLNNPSIETIYGNFNQFVSIFNTVTDVKKRLFE
|
Plays an essential role in viral DNA replication by acting as the polymerase processivity factor together with protein OPG116. Serves as a bridge which links the DNA polymerase OPG071 and the uracil DNA glycosylase.
|
A0A7H0DND1
|
PG160_MONPV
|
DNA packaging protein OPG160
|
MPSLFSSLLTTLVFHILIYYQINLVTVNIIMNCFQEKQFSRENLLKMPFRMVLTGGSGSGKTIYLLSLFSTLVKKYKHIFLFTPVYNPDYDGYIWPNHINFVSSQEALEYNLIRTKSNIEKCIAVAQNHKKSAHFLLIFDDVGDKLSKCNTLIEFLNFGRHLNTSIILLCQTYRHVPILGRANITHFCSFNISISDAENMLRSMPVKGKRKDILNMLNMIQTARSNNRLAIIIEDSVFCEGELRICTDTADKDVIEQKLNIDILVSQYSHMKKNLNTILESTKTKLCNSDQSSSSKNVSS
|
Participates in viral DNA packaging and virion morphogenesis.
|
A0A7H0DNF1
|
PG189_MONPV
|
Ankyrin repeat protein OPG189
|
MDFFKKEILDWSIYLFLHYITRLCSNSSNSSTSHIIQEYNLVRKYEKVDKTIVDFLSRWPNLFHILEYGENILHIYFIDAANTNIMIFFLDRVLNINKNRGSFIHNLGLSSINIKEYVYQLVNNDHLDNSIRLMLENGRRTRHFLSYILDTVNIYISILINHRFYIDAEDSYGCTLLHRCIYNYKKSESESYNELIKILLNNGSDVDKKDTYGNTPFILLCKHDIDNAELFEICLENANIDSVDFNGYTPLHYVSCRNKYDFVKLLISKGANVNARNRFGTTPFYCGIIHGISLIKLYLESDTELEIDNEHIVRHLIIFDAVESLDYLLSRGVIDINYRTIYNETSIYDAVSYNAYNTLVYLLNRNGDFETITTSGCTCISEAVANNNKIIMDILLSKRPSLKIMIPSMIAITKHKQHNADLLKMCIKYTACMTDYDTLIDVQSLHQYKWYILKCFDEIDIMKRCYIKNKTVFQLVFCIKDINTLMRYGRHPSFVKCNILDVYGSCVRNIIASIRYRQRLISLLSKKLDAGDKWSCFPNEIKYKILENFNDNELTTYLKIL
|
Contributes to viral release without involving rearrangement of host actin.
|
A0A7H0DNG0
|
PG200_MONPV
|
Protein OPG200
|
MTANFSTHVFSPQHCGCDRLTSIDDVRQCLTEYIYWSSYAYRNRQCAGQLYDTLLSFKDDAESVFIDVRELVKNMPWDNVKDCTEIIRCYIPDEQKTIREISAIIGLCAYAATYWGGEDHPTSNSLNALFVMLEMLNYMDYTIIFWRMN
|
Contributes to virulence by binding to the host IKBKB subunit of the IKK complex and preventing host NF-kappa-B activation in response to pro-inflammatory stimuli such as TNF-alpha or IL1B. Mechanistically, sterically hinders the direct contact between the kinase domains of IKBKB in the IKK complex containing IKBKB, CHUK/IKKA and NEMO.
|
A0A7H0DNG9
|
PG015_MONPV
|
Ankyrin repeat domain-containing protein OPG015
|
MESVDFMAVDEQFHDDLDLWSLSLVDDYKKHGLGVDCYVLEPVVDRKIFDRFLLEPICDPVDVLYDYFRIHRDNIDQYIVDRLFAYITYKDIISALVSKNYMEDIFSIIIKNCNSVQDLLLYYLSNAYVEIDIVDLMVDHGAVIYKIECLNAYFRGICKKESSVVEFILNCGIPDENDVKLDLYKIIQYTRGFLVDEPTVLEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGSVIARREAHLKILEILLREPLSIDCIKLAILNNTIENHDVIKLCIKYFMMVDYSLCNVYASSLFDYIIDCKQELEYIRQMKIHNTTMYELIYNRDKNKHASHILHRYSKHPVLTQCITKGFKIYTEVTEQVTKALNRRALIDEIINNVSTDDNLLSKLPLEIRDLIVSQAVI
|
May be involved in virus-host protein interaction through the ankyrin repeats.
|
A0A8D9PH56
|
OTO1_YEAST
|
Uncharacterized protein OTO1 (ORFan toxic when overexpressed protein 1)
|
MNVRGNQCIMSIRVFLKAGESSLSFAIKWLKRFEATTKKNQYIQNGWPLKDGNKKRK
|
Proetin of unknown function whose overexpression causes growth inhibition. Overexpression increases the expression of ergosterol synthesis genes.
|
A0AEY1
|
YABA_LISW6
|
Initiation-control protein YabA
|
MDKKAIFDSVSNMEEQIGELYQQLGDLKTNLGEMLEENNRLNLENEHLRRRLSLTDEGTLEPVAEEEAVHGVMAPNRKEAMQQMIELGEGYDNLVQLYKEGFHVCNVHFGSPRGNDEDCLFCLSLLNKK
|
Involved in initiation control of chromosome replication. {ECO:0000255|HAMAP-Rule:MF_01159}.
|
A0AJC4
|
YIDD_LISW6
|
Putative membrane protein insertion efficiency factor
|
MKKMLIGGIRLYQKYISRFTPATCRFYPTCSAYGIEAIETHGALKGSYLAIKRISKCHPFHKGGLDFVPPKKE
|
Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}.
|
A0AJQ7
|
Y1821_LISW6
|
UPF0122 protein lwe1821
|
MFEKTNRMNLLFDFYQELLTTKQKAYVSFYYLDDYSLGEIAEEFEVSRQAIYDNIKRTEESLEKYEEKLGMLKKYQQREKLFSELEAQLTKKNFLDEQVKDTLEQLKNID
|
Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein. {ECO:0000255|HAMAP-Rule:MF_00245}.
|
A0JMZ3
|
ZYG11_XENLA
|
Protein zyg-11 homolog
|
MEESSPKSLLDITLLYLSTHLEKFCWERQDGTYCLQDAAIFPQEVADRLLQAMAVQRQLNEVTVGIFRGNQLRLKRACIRKAKISAVAFRKAFCHHKLIELDATGVNADITITDIISGLSSSKWIRENLQCLVLNSLTLSLEDPYERCFSQLSGLRVLSITNVLFYNEDLADVASLPRLESLDISNTSVTDITALVACKDILKSLTMHHLKCLKMTTTQILEVIRELKKLNHLDMSDDKQFTSDIACRLLEQNDILLHLVSLDISGRKHVTDKAVEAFIRHRPQMQFVGLLATEAGYSEFLSGEGCVKVSGEANQTQIAEALRRYSERSFFVREALFHLFSLTHVMDKANPEMLKLVVIGMRNHPTNLPVQLAASACVFNLTKQDLAAGMPVKLLADVTHLLLEAMKHFPNHQQLQKNCLLSLCSDRILQDVPFNRFDAAKLVMQWLCNHEDQNMQRMAVAIISILAAKLSTEQTAQLGAELFIVRQLLQIVRQKTSQNMVDTTLKFTLSALWNLTDESPTTCRHFIENQGLELFMKVLETFPSESSIQQKVLGLLNNIAEVKELHTELMCKDFIDQISKLLHSVEVEVSYFAAGIIAHLVSRGEETWTLSSSMRETLLEQLHSAILSWPTPECEMVAYRSFNPFFPLLACFRTPGVQLWAVWAMQHVCSKNPVRYCSMLIEEGGLVRLHRIRDHMCADPDVLRITITILDNLDRHLKKHGNPPCQKPPFTK
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Serves as substrate adapter subunit in an E3 ubiquitin ligase complex zyg11-cul2-elongin BC. Targets substrates bearing N-terminal glycine degrons for proteasomal degradation.
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A0JPG1
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FHI2A_XENLA
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FHF complex subunit HOOK interacting protein 2A (FHIP2A)
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MFSKISSILQQAVEALAPSLPLQEDFVYHWKAITHYYIETSDDKAPVTDTNIPSHLEQMLDILVQEENERESGETGPCMEYLLHHKVLETLYTLGKADCPPGMKQQVLIFYTKLLGRIRQPLLPHINVHRPVQKLIRLCGEVLANPTENEEIQFLCIVCAKLKQDPYLVNFFLENKSKGAQSGGYIFPGGSAQHELLNDTGQPERTVGANADPGNESSSGDLKPSASSEASANHIQQDYNLVNSLLNLTKSPDGRIAVKACEGLMLLVSLPEVAAAKCLTQSTSLCQLLTDRLTSLYQALPHSIDPLDIETVEGINWGLDSYSVKEDASAFPGKRALISFLSWFDYCDQLIKEAHRIAASAMARSVRERFLVGIMEPQLLQTSEIGILTATALLHRIVRQVTSKSLLEQIVYFILGEHRDPETLRDVHKTPLRHRLIEHCNHISDEISIMTLRLFEHLLHKPNEHILYNLVLRNLEERNYTEYKPPCPEDKDIVENGQIPGAVDLEEDPIFTGMSPENTLSKEWLSASPPITPEHHRTDGKTEVHKIVNSFLCLVPDEAKSSYQVEGTGYDTYLRDAHRQFREYCAICLRWDWPGAAKAIDKCNLEAPFFEGHFLKVLFDRMGRILDQPYDVNLQVTSVLSKLSLFPHPHIHEFLLDPYVNLAPGCRSLFSVIVRVVGDLMVRIQRIPEFTPKLLLVRKRLLGLEPDGPMVDHMTLLEGVIVLEEFCKELAAIAFVKYHSSSTP
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May be required for proper functioning of the nervous system.
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A0K4S1
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HRCA_BURCH
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Heat-inducible transcription repressor HrcA
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MLDPRARTLLKTLIERYIADGQPVGSRTLSRYSGLELSPATIRNVMSDLEELGLVSSPHTSAGRVPTPRGYRLFVDTMLTVEAPIDAEAVARQVQNTLQAGEPQQRVVAAAASVLSNLSQFAGVVLTPRRSHVFKQIEFMRLSDKRILLIIVTPEGDVQNRMLATPRDYSPSQLTEASNYINAHFAGLSFDEVRRRLRDEIDQLRGDMTTLMHAAVTASTEVPDTEDTVLISGERNLLEVADLSSDMARLRKLFDVFDQKTGLLQLLDVSSHAQGVQIFIGGESTLVPIEEMSVVTAPYEVNGQIVGTLGVIGPTRMAYNRVIPIVDITARLLSLTLSQQ
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Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons. {ECO:0000255|HAMAP-Rule:MF_00081}.
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A0K8T1
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FETP_BURCH
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Probable Fe(2+)-trafficking protein
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MARMIQCAKLGKEAEGLDFPPLPGELGKRIYESVSKEAWQGWLKQQTMLINENRLNMADPRARQYLMKQTEKYFFGDGADQASGYVPPTEG
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Could be a mediator in iron transactions between iron acquisition and iron-requiring processes, such as synthesis and/or repair of Fe-S clusters in biosynthetic enzymes. {ECO:0000255|HAMAP-Rule:MF_00686}.
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A0KBN4
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YIDD_BURCH
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Putative membrane protein insertion efficiency factor
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MKTVLIALLRFYKVAVSPMLGNRCRFYPSCSDYAREAIQYHGAARGTYLAVRRVCRCHPFSAGGVDLVPPPNSDTRARGEADARSHRL
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Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}.
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A0KHE8
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SYDP_AERHH
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Protein Syd
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MSDQVLSALEHFFLRWQRDGEARRGLPLCEWEADWRSPCELDEPKEGRVAWRPHRRAEPADFTAMNEALELTLHPAAQALFGGWFSRPVPCLYKGLRLEFVLPWNEADLDLLKENLIGHLLMLRKLKRSPSLFIATTRNEMTLVSLDNESGQVWLEWLDSGRRLVLAPSLPAFLERLETLPQ
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Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function. {ECO:0000255|HAMAP-Rule:MF_01104}.
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A0KPN5
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FETP_AERHH
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Probable Fe(2+)-trafficking protein
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MSRTVFCQRLKKEGPGLDFQLYPGELGKRIFDNISKEAWTEWQKKQVMLINEKKLNMMNLEHRQLLEKEMVNYLFEAGEVAIDGYTPPSK
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Could be a mediator in iron transactions between iron acquisition and iron-requiring processes, such as synthesis and/or repair of Fe-S clusters in biosynthetic enzymes. {ECO:0000255|HAMAP-Rule:MF_00686}.
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A0KR33
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YIDD_SHESA
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Putative membrane protein insertion efficiency factor
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MAQTQSPLQWLATTFIRGYQIFISPLLGPRCRFNPTCSHYAIEAIKVHGTAKGCWFALKRILKCHPLHPGGSDPVPPKNDRCNK
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Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}.
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A0KUE6
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FETP_SHESA
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Probable Fe(2+)-trafficking protein
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MARTVNCVYLNKEADGLDFQLYPGDLGKRIFDNVSKEAWGLWQKKQTMLINEKKLNMMNVDDRKFLEEQMTSFLFEGKDVEIEGFVPEKGQE
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Could be a mediator in iron transactions between iron acquisition and iron-requiring processes, such as synthesis and/or repair of Fe-S clusters in biosynthetic enzymes. {ECO:0000255|HAMAP-Rule:MF_00686}.
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A0L6W5
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COWN_MAGMM
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N(2)-fixation sustaining protein CowN (CO weal-nitrogenase)
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MNTPAARPDRYQSFAHIPCDAMALKLLTHLEQLLQAEDTLEPFWQLFLQKAAIAKQPQPGQADALKLICSNSYYIFDLFAAQQDQAGEAMMDELEYQCC
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Is required to sustain N(2)-dependent growth in the presence of low levels of carbon monoxide (CO). Probably acts by protecting the N(2) fixation ability of the nitrogenase complex, which is inactivated in the presence of CO. {ECO:0000255|HAMAP-Rule:MF_02117}.
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A0LE50
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YIDD_MAGMM
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Putative membrane protein insertion efficiency factor
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MGRLLVLLVRFYQLFISPVLPPSCRHSPTCSQYAIEALQKHGAIKGSWLAFRRVLRCNPWHPGGYDPVP
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Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}.
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A0LLH2
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YIDD_SYNFM
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Putative membrane protein insertion efficiency factor
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MIRSIFLGLIRFYQIVLSPLKGPRCRFLPTCSQYAYEAIERYGIWRGLFLGGKRLLRCHPFHAGGYDPVPRPSANNHPSR
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Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}.
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A0MFL4
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LOR17_ARATH
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Protein LURP-one-related 17
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MFPFLKQRSRSVHGEDAPSSTESTVSVAAADIGGACTTLTVWRKSLLVSCEGFTVIDSNGDLIYRVDNYARTRPEELILMDKDGNSLLLMHRTKKITLVDSWGIYEANDTKGETKIPKCPTWYMRKNLKMNILSTKSDILAYVYSGSFDKKNSYIIKGSYRCKSCKIVHVPLNKTVVEIKRKEVRTKGVRFGSDVFDLVVNPGFDTGLAMALVLLLDQMFS
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Might be related to the phospholipid scramblase and tubby-like superfamily of membrane tethered transcription factors.
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A0MZA0
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GP8_BPN4
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Gene product 8 (gp8)
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MEQLNYGYKIKRNQVRGSWLFLVYGKPIYELHRGEKSKTYYVTHIATGKTPACAGLLRDAIMKACMLEGLL
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Targets the host DNA sliding clamp and inhibits host DNA replication.
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A0PTU2
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HRCA_MYCUA
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Heat-inducible transcription repressor HrcA
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MGTADERRFEVLRAIVADFVATHEPIGSKSLVERHNLGVSSATIRNDMAVLEAEGYIAQPHTSSGRVPTEKGYREFVDRLDDVKPLSMVERRAIQGFLESGVDLDDVLRRAVRLLAQLTRQVAVVQYPTLSTSKVRHLEVIALTPARLLVVVITDSGRVDQRIVELGDVIDDHQLSQLRELLGQALEGKKLAAASVAVADFAGQLSGAGGLGDAVGRSATVLLESLVEHTEERLLMGGTANLTRNAADFGGSLRSILEALEEQIVVLRLLAAQQEAGKVTVRIGHETEAEQIVGTSMVSTAYGSNDTVYGGMGVLGPTRMDYPGTIASVAAVALYIGEVLGAR
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Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons. {ECO:0000255|HAMAP-Rule:MF_00081}.
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A0PX74
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YIDD_CLONN
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Putative membrane protein insertion efficiency factor
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MLKIILIHIIKFYRKYISPLKKPCCRFYPTCSKYALDAINKYGAFKGSIMAIKRILRCHPFNPGGYDPVK
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Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}.
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A0PXK7
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SP5G_CLONN
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Putative septation protein SpoVG
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MQITDVRIRKISAEGKMKAIVSVTFDNEFVVHDIKVIEGQNGLFIAMPSRKTPTGEFKDIAHPINTETRQKIQKAILDEYEVVKNETTNNENGEEITSED
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Could be involved in septation. {ECO:0000255|HAMAP-Rule:MF_00819}.
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A0Q0Y5
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Y2214_CLONN
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UPF0122 protein NT01CX_2214
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MEDRIKISILMDYYRELLTEKQKYVMELYFNQDLSLAEISELTNTSRQAIYDIIKRCNKLLVDYEKKLNLARKNKELIKAKQIIIEKINDLEYSNNKNDFKNSLEDIKNTIVQYI
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Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein. {ECO:0000255|HAMAP-Rule:MF_00245}.
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A0Q420
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YIDD_FRATN
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Putative membrane protein insertion efficiency factor
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MFFKKITLIPFVMLINLYRYCISPFIPARCRYYPTCSEYALEALKTHGILKGLYLTTRRLLRCHPLSKRDYYDPVPCKNKKG
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Could be involved in insertion of integral membrane proteins into the membrane. {ECO:0000255|HAMAP-Rule:MF_00386}.
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A0Q5C7
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FETP_FRATN
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Probable Fe(2+)-trafficking protein
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MTKVFCKKYHQELDAIPFQPLPGELGKKIHNEISNKAWQAWLAHQTILINEYRLNLIEPKAKEFLKEEMHKFLFEGKEEKPEQFSEI
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Could be a mediator in iron transactions between iron acquisition and iron-requiring processes, such as synthesis and/or repair of Fe-S clusters in biosynthetic enzymes. {ECO:0000255|HAMAP-Rule:MF_00686}.
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A0QEA3
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HRCA_MYCA1
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Heat-inducible transcription repressor HrcA
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MGSADERRFEVLRAIVADFIATKEPIGSKTLVERHNLGVSSATVRNDMAVLEAEGYITQPHTSSGRVPTEKGYREFVDRLDDVKPLSAAERRAIQNFLESGVDLDDVLRRAVRLLAQLTRQVAIVQYPTLSSSTVRHLEVIALTPARLLMVVITDSGRVDQRIVELGDVIDDHELSRLREMLGQALVGKKLSAASVAVADLAEQLRSPDGLGDAVGRSATVLLESLVEHSEERLLMGGTANLTRNAADFGGSLRSILEALEEQVVVLRLLAAQQEAGKVTVRIGYETAAEQMVGTSMVTTAYGTSDTVYGGMGVLGPTRMDYPGTIASVAAVAMYIGEVLGAR
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Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons. {ECO:0000255|HAMAP-Rule:MF_00081}.
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