msl3

Mycolipanoate synthase

2085 amino acids

Polyketide synthase involved in the biosynthesis of methyl-branched fatty acids such as mycolipanoic, mycolipenic (phthienoic) and mycolipodienoic acids required for the synthesis of a major class of polyacylated trehaloses. Catalyzes the elongation of CoA esters of long-chain fatty acids by incorporation of three methylmalonyl (but not malonyl) residues, to form trimethyl-branched fatty-acids.

220.462 kDa

MRTATATSVAVIGMACRLPGGIDSPQRLWEALLRGDDLVGEIPADRWDANVYYDPEPGVPGRSVSRWGAFLDDVGGFDCDFFGLTEREATAIDPQHRLLLEVSWEAIEHAGVDPATLAESQTGVFVGLTHGDYELLSADCGAAEGPYGFTGTSNSFASGRVAYTLGLHGPAVTVDTACSSGLTAVHQACRSLDDGESDLALAGGVVVTLEPRKSVSGSLQGMLSPTGRCHAFDEAADGFVSGEGCVVLLLKRLPDAVRDGDRVLAIVRGTAANQDGRTVNIAAPSAQAQIAVYQQALAAAGVEASTVGMVEAHGTGTPVGDPVEYASLAAVYGTEGPCALTSVKTNFGHLQSASGPLGLMKTILALRHGVVPQNLHFCRLPDQLAEIDTELFVPQANTSWPDNTGQPRRAAVSSYGMSGTNVHAILEQAPVSEPAASGPELTPEAGGLALFPVSATSAEQLHVTAARLADWVDQNGNAGSRVSMRDLGYTLSCRRAHRPVRTVVTASSFDELSAALRDVAGDQIPYQPAVGHDDRGPVWVFSGQGSQWPGMGTELLVAEPVFAATVAAMEPVIARESGFSVTEAMSAPQTVSGIDRVQPTIFAVQVALAAALKSYGVRPGAIIGHSLGEAAAAVVAGALSLHDGLRVICRRSRLMSRIAGSGAMASVELPGQQVLSELAIRGISDVVLSVVASPTSTVVGGATQSIRDLVAAWEQQDVLAREVAVDVASHTPQVDPILDELLEVLAEVDPTAPEIPYYSATLWDPRERPSFTGEYWVENLRYTVRFAAAVQAALKDGYRVFGELAPHPLLTYAVEQNAASLDMPIATLAAMRRGEQLPFGLRGFVADVHNAGAKVDFSVQYPDGRLVDAPLPSWTHRTLMLSREDSHRSHTGAVQAVHPLLGAHVHLLEEPERHVWQAGVGTGAHPWLGDHRIHNVAAFPGAAYCEMALAAARTTLGELSEVRDIKFEQTLLLDEQTVVSSAATIAAPGILQFAVESHQEGEPARRASAMLHALEEMPQPPGYDTNALTAAHESSMSGEELRKMFNSLGIQYGPAFSGLVAVHTARGDVTTVLAEVALPGAIRSQQSAYASHPALLDACFQSVLVHPEVQKATVGGLMLPVGVRRLRNYHSTRSAHYCLARVTSSSRAGECEADLDVFDQAGTVLLTVEGLRLAAGISEHERANRVFDERLLTIEWERGELPEVPQIDAGSWLLLSASEADPLTAQLADALNAVGAQSTSVASASDVAQLRSLLGGRLTGVVVVTGPPTGGLTQCGRDYVSQLVGIARELAELPGEPPRLFVVTRSAASVLPSDLANLEQAGLRGLMRVIDSEHPHLGATAIDVDNDETVAALVASQLQSGSQEDETAWRNGIWYTARLRPGPLRPAERRTAVVEYRRDGMRLQIRTPGDLESLEFVTFDRVAPGPGEIEVAVTASSVNFADVLVAFGRYPTFEGYRQQLGIDFAGVVTAVGPDVTEHRIGDHVGGMSANGCWSTFVRCDARLAVTLPPELPVAAAAAVPTASATAWYALHDLARICSDDKVLIHSGTGGVGQAAIAIARAAGCEIFATAGSAQRRQLLHDMGVEHVYDSRSTEFAEQIRGDTDGYGVDVVLNSLPGAAQRAGIELLAFGGRFVEIGKRDIYGDTRLGLFPFRRNLSLYAVDLALLTHSHPHTVRRLLKTVYQHTVEGTLPVPQTTHYPIHDAAVAIRLVGGAGHTGKVVLDVPRTGEGVAVVPPEQVRTSRPDGAYLVTGGLGGLGLFLAGELAAAGCGRIVLNSRSTPSPHATRVIERLRAAGADIQVECGDIADAATAHRVVAVATASGLPVRGVLHAAAVVEDATLANVTDELIDRCWAPKVHGAWNIHRATAAQPLEWFCLFSSAAALVGSPGQGAYAAANSWLDAFAHWRRAQGLPATSIAWGAWAEIGRATALAEGTGAAIAPAEGARAFQTLLRYGRAYSGYAPIMGTPWLTAFAQRSRFAEAFHATGQNQPATGKFLAELGSLPREEWPRTVRRLVSDQISLLLRRTIDPDRPLSDYGLDSLGNLELRTRIETETGIRVSPTKITTVRGLAEHVCDELAAAQSAPV

MSL3

Mechanosensitive ion channel protein 3, chloroplastic

678 amino acids

Mechanosensitive channel that opens in response to stretch forces in the membrane lipid bilayer. Controls plastid size, shape, and perhaps division during normal plant development by altering ion flux in response to changes in membrane tension. Acts as a component of the chloroplast division machinery.

Belongs to the MscS (TC 1.A.23) family.

74.189 kDa

MMMRTVALPLSHDLNVHKIHEASGFHNSAAGKNRVYLTRTGLSSCATRQDVWSLQLLESLSGSIVPVSSRCNAFVCRSALSPGNGNEGPILKSTAVIFTRVYDALGGNPHLVKLIPAVGILAFATWGLRPLLRLARTTLFEKGNDANSQKSSTQYIVVSYLQPLLLWSGAILLCRTLDPIVLPSSAGQAIKQRLLIFARSISTVLAFSCCLSSLLQQVQKFFMETNNPADTRNMGFSFAGKAVYTAAWVAAASLFMELLGFSTQKWLTAGGLGTVLLTLAGREILTNFLSSIMIHATRPFVLNEWIQTKIGGYEVSGTVEQVGWWSPTIIRGDDREAVHIPNHQFSVNIVRNLTQKTHWRIKTHLAISHLDVSKINNIVADMRKVLSKNPQIEQQKIHRRVFLEDIDPENQALRILISCFVKTSRFEEYLCVKEAVLLDLLTVIRHHGARLATPIRTVQRMRNEAEVDTAGFSDIVFNQAAMNRRYMLIEPSYKINSDDNSKSPSPSPGQKSPSPGQKSEERDLQEEPSETKAETENNGSVPVSNAKKENQKAALGSNSNTGTKGSSTSTSDQPVAQKSEEKKKESVGDPHKAEKDEVSDDEATIEQTLKSKAKQGSEKNNGESKARDGGGSGTSSLLEENLVLGVALDGSKRTLPIDEEHKASGALMDSEELGIGSE

Msl3

Male-specific lethal 3 homolog

525 amino acids

Has a role in chromatin remodeling and transcriptional regulation. Has a role in X inactivation. Component of the MSL complex which is responsible for the majority of histone H4 acetylation at 'Lys-16' which is implicated in the formation of higher-order chromatin structure. Specifically recognizes histone H4 monomethylated at 'Lys-20' (H4K20Me1) in a DNA-dependent manner and is proposed to be involved in chromosomal targeting of the MSL complex.

60.292 kDa

MSASEGMKFQFHSGEKVLCFEPDPTKARVLYDAKIIDVIIGKDEKGRKIPEYLIHFNGWNRSWDRWAAEEHVLHDTDENRRLQRKLAKKAIARLRGTGKKKRRCRLPGVDSVLKSVPVKEKSKNDENSVSSTCHESCGEKNGGIKEHRQRRIKVKAKAKKKVLSLRSRKEMDERTITIDIPDVLKKQLEDDCYYINRRKRLVKLPCQTNIITILESYVKHFAINAAFSANERPRHHHAMMHTHMNVHYVPAEKNVDLCKEMVDGLRITFDYTLPLVLLYPYEQTQYKRVTSSKFFLPIKESTTTTNRSQEELSPSPPLLNPSTPQSTESQPPTGEPATPKRRKAEPEALQSLRRSTRHSTNCDRLSESSSSPQPKRRQQDTSASMPKLFLHLEKKTPVHSRSSSPIPLTPSKDGSAVFAGFEGRRPNEINEVLSWKLVPDNYPPGDQPPPPSYIYGAQHLLRLFVKLPEILGKMSFSEKNLKALLKHFDLFLRFLAEYHDDFFPESAYVAACEAHYSTKNPRAIY

MSL3

Male-specific lethal 3 homolog

521 amino acids

Has a role in chromatin remodeling and transcriptional regulation (PubMed:20018852, PubMed:20657587, PubMed:20943666, PubMed:21217699). Has a role in X inactivation (PubMed:21217699). Component of the MSL complex which is responsible for the majority of histone H4 acetylation at 'Lys-16' which is implicated in the formation of higher-order chromatin structure (PubMed:16227571, PubMed:20657587, PubMed:16543150). Specifically recognizes histone H4 monomethylated at 'Lys-20' (H4K20Me1) in a DNA-dependent manner and is proposed to be involved in chromosomal targeting of the MSL complex (PubMed:20657587, PubMed:20943666).

59.824 kDa

MSASEGMKFKFHSGEKVLCFEPDPTKARVLYDAKIVDVIVGKDEKGRKIPEYLIHFNGWNRSWDRWAAEDHVLRDTDENRRLQRKLARKAVARLRSTGRKKKRCRLPGVDSVLKGLPTEEKDENDENSLSSSSDCSENKDEEISEESDIEEKTEVKEEPELQTRREMEERTITIEIPEVLKKQLEDDCYYINRRKRLVKLPCQTNIITILESYVKHFAINAAFSANERPRHHHVMPHANMNVHYIPAEKNVDLCKEMVDGLRITFDYTLPLVLLYPYEQAQYKKVTSSKFFLPIKESATSTNRSQEELSPSPPLLNPSTPQSTESQPTTGEPATPKRRKAEPEALQSLRRSTRHSANCDRLSESSASPQPKRRQQDTSASMPKLFLHLEKKTPVHSRSSSPIPLTPSKEGSAVFAGFEGRRTNEINEVLSWKLVPDNYPPGDQPPPPSYIYGAQHLLRLFVKLPEILGKMSFSEKNLKALLKHFDLFLRFLAEYHDDFFPESAYVAACEAHYSTKNPRAIY

MSL3

Male-specific lethal 3 homolog

521 amino acids

May be involved in chromatin remodeling and transcriptional regulation. May have a role in X inactivation. Component of the MSL complex which is responsible for the majority of histone H4 acetylation at 'Lys-16' which is implicated in the formation of higher-order chromatin structure. Specifically recognizes histone H4 monomethylated at 'Lys-20' (H4K20Me1) in a DNA-dependent manner and is proposed to be involved in chromosomal targeting of the MSL complex (By similarity).

59.81 kDa

MSASEGMKFKFHSGEKVLCFEPDPTKARVLYDAKIVDVIVGKDEKGRKIPEYLIHFNGWNRSWDRWAAEDHVLRDTDENRRLQRKLARKAVARLRSTGRKKKRCRLPGVDSVLKGLPTEEKDENDENSLSSSSDCSENKDEEISEESDIEEKTEVKEEPELQTRREMEERTITIEIPEVLKKQLEDDCYYINRRKRLVKLPCQTNIITILESYVKHFAINAAFSANERPRHHHVMPHANMNVHYIPAEKNVDLCKEMVDGLRITFDYTLPLVLLYPYEQAQYKKVTSSKFFLPIKESATSTNRSQEELSPSPPLLNPSTPQSTESQPTTGEPATPKRRKAEPEALQSLRRSTRHSANCDRLSESSASPQPKRRQQDTSGSMPKLFLHLEKKTPVHSRSSSPIPLTPSKEGSAVFAGFEGRRTNEINEVLSWKLVPDNYPPGDQPPPPSYIYGAQHLLRLFVKLPEILGKMSFSEKNLKALLKHFDLFLRFLAEYHDDFFPESAYVAACEAHYSTKNPRAIY