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helA

Gene
helA
Protein
ATP-dependent RNA helicase ddx54
Organism
Dictyostelium discoideum
Length
1091 amino acids
Function
ATP-binding RNA helicase which may be involved in the ribosome biogenesis.
Similarity
Belongs to the DEAD box helicase family. DDX54/DBP10 subfamily.
Mass
125.085 kDa
Sequence
MVKPNNVKIKNKGNLKKSNESQNDYMKGKKLETKSYQKALLSKNSNNNNDGAQAKRLKKKEEFKKKLEKRQNTIVIKDKLKEPSTFLKEDQSFFDQNIFNDQDDYKHQQMNRININENFETNLFGDMMNEFDGDLNEDLDLLDYNDEVIDNSNFDNNGDQFNSEDEEFYDDEKQAKKSNKNKNADADNKKSKKSNKKEEIESSEKFESFPMDENNEQEEETTSKKKKKTGGFQSMDLTKNLLKAILKKGFNVPTPIQRKSIPMILDGHDIVGMARTGSGKTGAFVIPMIQKLGDHSTTVGVRAVILSPTRELAIQTFKVVKDFSQGTQLRTILIVGGDSMEDQFTDLARNPDIIIATPGRLMHHLLETGMSLSKVQYIVFDEADRLFEMGFNEQLTEILSKLSENRQTLLFSATLPSLLVDFVRAGLNNPKLINLDTDTKISENLSLSFFTLRHEEKLGVLLFLLKDIIYKKPQLPTTETTTTTTTNNESNQQQQKKSSTIIFVSTKYHVEFIHILLERAGIASTYIHGYLDPVARKINLAKFRSHQVGVMVVTDLAARGIDIPLLDNVINFDFPPKEKIFIHRVGRVARAGRSGIAYSLVSPDEVPYMIDLHLYLGRKFLNKFQYEGQTINDPKYSFYGTIPQTIIDRETEFVNVQRKECIELLSLTKTIHNAHKKYLSTRPGASHESNRRAKLMDKSKYHPMLSDHLNSNDQIRNDFIQSLKSFRPPQTVLELDARKNNVQVSIMKDKRKVHTNVIESQQKKLYLQQSETNLGPENEEFDYSKLDTRKRLLQLTENITEEMLRSNKSNDNNDNNKDIKMNENDDENDDDDEEGENDDDEEEENEKDEDDEEDENKNKFNIKIESSDKNDNNKKKLKSRSSSRDPNFFISATPENLIQERAMSISNRFTKDDEVNLVADTDRKQKKSMVWDKRKGKFVSSQADADRKNSKKLVRNEAGKLVEAKKSHKGYEEWKKKTHGRIQRVGEDENSKYQPNQKEYLPQKWRGQGREKEKKDNKASHAKGSHGLKGRPSELKDKNQISKNRSEKERKMRVNKTKGNPKGSKSKSGGGGGGKGSKFGSGKSKGGKSRK

Gene
helA
Protein
Protein HelA
Organism
Legionella pneumophila
Length
1052 amino acids
Function
Presumed to function with HelC and HelB in efflux of an unidentified substrate.
Similarity
Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family.
Mass
115.821 kDa
Sequence
MLEKIIRFSLKHRWFVLLFTLVIAILGVYNFQRLPIDAVPDITNVQVQINTQASGYSPFEVEQRITFPIELAMSGLPSLDYTRSLSRYGLSQVTVVFKDGTNIYFARQLINERLQEVKDKLPPGVETTLGPISTGLGEIFMYTVTNKPNVPISQHYNPTELRTIQDWIIKPQLRNVEGVAEVNTIGGYEKQFHITPDPSKLVRYRLSLNDVVEALERNNANVGAGYIETNGEQNLIRVPGQVQNMADIENIVIASFEGTPVRIRDVAEVALGKELRTGAATENSKEVVLGTVFILMGENSRTVSERVAAKMKDINKTLPEGVEAITVYNRTTLVNATINTVKNNLLEGALLVCVILFLFLGNIRAALITAMVIPLSMLLTITGMVENQISANLMSLGALDFGLIVDGAVIIVENCIKHLAEQQHALHRVLNLEERLKVISYATTEVIRPSIFGVFIITVVYLPILTLTGVEGKMFLPMAQTVIIALLASMLFALTFVPAAVAIFLRGHLQEKENWLVHYLSLGYAKVLRRCFHARRVVISAAVALVVVSLGIAFHLGGEFIPSLDEGDIAMHAMRIPGTSLTQAITMQDLVEKRIRQFSEVKNVFAKLGTAEVATDPMPPNVADTFIILKSRKKWTNPKKTKPGLVQEIESAVQQIPGNNYEFTQPIQMRFNELISGVRSDVAVKVFGDDMDTLLKTAEAISAQLKQVPGAADVKVEQVSGLPLLTVEINRDVLARYGLQIGTVQEAVVIATGGKKGGELFEGDKRFDIVVRLPESLRSDPNVLRQIFIPLPLSKDGEQHFIPLSEVASLIRSESPNQISRENGKRRVVVTANVRNRDLSSFVSEAKKRIDGQVKLPSGYWITWGGQFEQLQSAYQRLQIVVPITLLGIFLLLFISFGKVRDALLVFTGIPLALTGGVFALWLRGIPLSISAGVGFIALSGVAVLNGLVMITFINKLREQKKVYLKDAVLQGSLARLRPVLMTALVASLGFVPMALATGTGSEVQRPLATVVIGGIISSTFLTLLVLPGLYYVFHGRRKKGQSKSEPQEQIM

Gene
helA
Protein
Protein HelA
Organism
Legionella pneumophila
Length
1052 amino acids
Function
Presumed to function with HelC and HelB in efflux of an unidentified substrate.
Similarity
Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family.
Mass
115.821 kDa
Sequence
MLEKIIRFSLKHRWFVLLFTLVIAILGVYNFQRLPIDAVPDITNVQVQINTQASGYSPFEVEQRITFPIELAMSGLPSLDYTRSLSRYGLSQVTVVFKDGTNIYFARQLINERLQEVKDKLPPGVETTLGPISTGLGEIFMYTVTNKPNVPISQHYNPTELRTIQDWIIKPQLRNVEGVAEVNTIGGYEKQFHITPDPSKLVRYRLSLNDVVEALERNNANVGAGYIETNGEQNLIRVPGQVQNMADIENIVIASFEGTPVRIRDVAEVALGKELRTGAATENSKEVVLGTVFILMGENSRTVSERVAAKMKDINKTLPEGVEAITVYNRTTLVNATINTVKNNLLEGALLVCVILFLFLGNIRAALITAMVIPLSMLLTITGMVENQISANLMSLGALDFGLIVDGAVIIVENCIKHLAEQQHALHRVLNLEERLKVISYATTEVIRPSIFGVFIITVVYLPILTLTGVEGKMFLPMAQTVIIALLASMLFALTFVPAAVAIFLRGHLQEKENWLVHYLSLGYAKVLRRCFHARRVVISAAVALVVVSLGIAFHLGGEFIPSLDEGDIAMHAMRIPGTSLTQAITMQDLVEKRIRQFSEVKNVFAKLGTAEVATDPMPPNVADTFIILKSRKKWTNPKKTKPGLVQEIESAVQQIPGNNYEFTQPIQMRFNELISGVRSDVAVKVFGDDMDTLLKTAEAISAQLKQVPGAADVKVEQVSGLPLLTVEINRDVLARYGLQIGTVQEAVVIATGGKKGGELFEGDKRFDIVVRLPESLRSDPNVLRQIFIPLPLSKDGEQHFIPLSEVASLIRSESPNQISRENGKRRVVVTANVRNRDLSSFVSEAKKRIDGQVKLPSGYWITWGGQFEQLQSAYQRLQIVVPITLLGIFLLLFISFGKVRDALLVFTGIPLALTGGVFALWLRGIPLSISAGVGFIALSGVAVLNGLVMITFINKLREQKKVYLKDAVLQGSLARLRPVLMTALVASLGFVPMALATGTGSEVQRPLATVVIGGIISSTFLTLLVLPGLYYVFHGRRKKGQSKSEPQEQIM

Gene
helA
Protein
Protostadienol synthase helA
Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
Length
735 amino acids
Function
Protostadienol synthase; part of the gene cluster that mediates the biosynthesis of helvolic acid, an antibacterial nortriterpenoid (PubMed:19415934, PubMed:19216560, PubMed:19951700, PubMed:29158519). Protostadienol synthase helA cyclizes (3S)-oxidosqualene to (17Z)-protosta-17(20),24-dien-3-beta-ol (protostadienol)(PubMed:19415934, PubMed:19216560, PubMed:19951700, PubMed:29158519). The synthesis of protostadienol is followed by several steps of monooxygenation, dehydrogenation, and acyl transfer to yield the final helvolic acid (PubMed:19216560). Following the cyclization to the tetracyclic protostadienol by helA, cytochrome P450 monooxygenases helB1-mediated and helB2-mediated oxidation at C-4 and C-16, acyltransferase helD2-dependent acetylation of 16-OH, oxidation of C-21 by cytochrome P450 monooxygenase helB4, and short chain dehydrogenase helC-dependent oxidative decarboxylation yield the fusidane skeleton (PubMed:29158519). This intermediate is further modified in three additional steps mediated by the cytochrome P450 monooxygenase helB3, the acyltransferase helD1, and the 3-ketosteroid 1-dehydrogenase helE to give helvolic acid (PubMed:19415934, PubMed:19216560, PubMed:29158519). Compared with the late stages in the biosynthesis of helvolic acid, enzymes involved in the early stage modifications act in a relatively strict order (PubMed:29158519). The hydroxylation of C-16 by helB1 and subsequent acetylation by helD2 should occur before the helB3-mediated oxidation of C-21 (PubMed:29158519). C-4 demethylation in fusidane-type antibiotics proceeds in an unusual manner though it is also achieved by oxidative decarboxylation (PubMed:19415934, PubMed:29158519). The methyl group at C-4 beta position is oxidized by helB1 and subsequently removed by the short chain dehydrogenase helC (PubMed:19415934, PubMed:29158519).
Similarity
Belongs to the terpene cyclase/mutase family.
Mass
83.091 kDa
Sequence
MATDSSMPGTVIGKAEFSDTKAASEFGTDLSRWRLNVDNGRHMWEYLESEDEARKRPQSFLEKYWLGLPYELPARPRATCALEAVENGWEFFKRLQTADGHWGCNDDGPLFVTSGMVIARYIVGIPIDSHMKQEMCRYLLNVVNEDGGWGLFIQSPSTVFGTVMNYCMLRILGLGPEHPAMAKARNTLHRLGSARATPTWGKFWLCVLGVYEWEGMVPLPPEPLLVPASLPFNPGKWWVHTRNVYISMSYLYGHRFSMPPNKLVQALRDELYDIPYQQINWPAQRTNVSAADRLTDPTWIQRSFTSALTMYETFKIPFLRRRALNEALFQIETETRNTHYLCIAPVSFASNMLALYHAHGRDSHWIRGMRDRFIDPMWLCREGLAASGTNGTSLWDTALTVQATIDAGLAARPENQAILRKALEFIDNSQIREDPLGVHHVYRQPTRGAWPFSTRDQSYAVSDTTAEAVKVIVLLQRIEGFPSRISDERLQQAIDLILGMENAGGGFSAYEPVRGPKFLELLNITELYENVMTDNLYPECTSSVIMCLTTFAREYPTYRPRDIQACLSRSIDYLLRSQYPNGGWFASWGVCFTYATMFALQGLACMGWNESNCAACQRACSFLLQHQNPDGGWGESLDTVRFKQYLPHPDGSQVTNTAYAVIGLLAARCGNHEAIRRGVAYLVKEQQDTGEWLPGPLEGVFAPPGGMRYPNYKFHFTLMALGRYVAIHGNECLAI

Gene
helA
Protein
Protostadienol synthase helA
Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
Length
735 amino acids
Function
Protostadienol synthase; part of the gene cluster that mediates the biosynthesis of helvolic acid, an antibacterial nortriterpenoid (PubMed:19415934, PubMed:19216560, PubMed:19951700, PubMed:29158519). Protostadienol synthase helA cyclizes (3S)-oxidosqualene to (17Z)-protosta-17(20),24-dien-3-beta-ol (protostadienol)(PubMed:19415934, PubMed:19216560, PubMed:19951700, PubMed:29158519). The synthesis of protostadienol is followed by several steps of monooxygenation, dehydrogenation, and acyl transfer to yield the final helvolic acid (PubMed:19216560). Following the cyclization to the tetracyclic protostadienol by helA, cytochrome P450 monooxygenases helB1-mediated and helB2-mediated oxidation at C-4 and C-16, acyltransferase helD2-dependent acetylation of 16-OH, oxidation of C-21 by cytochrome P450 monooxygenase helB4, and short chain dehydrogenase helC-dependent oxidative decarboxylation yield the fusidane skeleton (PubMed:29158519). This intermediate is further modified in three additional steps mediated by the cytochrome P450 monooxygenase helB3, the acyltransferase helD1, and the 3-ketosteroid 1-dehydrogenase helE to give helvolic acid (PubMed:19415934, PubMed:19216560, PubMed:29158519). Compared with the late stages in the biosynthesis of helvolic acid, enzymes involved in the early stage modifications act in a relatively strict order (PubMed:29158519). The hydroxylation of C-16 by helB1 and subsequent acetylation by helD2 should occur before the helB3-mediated oxidation of C-21 (PubMed:29158519). C-4 demethylation in fusidane-type antibiotics proceeds in an unusual manner though it is also achieved by oxidative decarboxylation (PubMed:19415934, PubMed:29158519). The methyl group at C-4 beta position is oxidized by helB1 and subsequently removed by the short chain dehydrogenase helC (PubMed:19415934, PubMed:29158519).
Similarity
Belongs to the terpene cyclase/mutase family.
Mass
83.091 kDa
Sequence
MATDSSMPGTVIGKAEFSDTKAASEFGTDLSRWRLNVDNGRHMWEYLESEDEARKRPQSFLEKYWLGLPYELPARPRATCALEAVENGWEFFKRLQTADGHWGCNDDGPLFVTSGMVIARYIVGIPIDSHMKQEMCRYLLNVVNEDGGWGLFIQSPSTVFGTVMNYCMLRILGLGPEHPAMAKARNTLHRLGSARATPTWGKFWLCVLGVYEWEGMVPLPPEPLLVPASLPFNPGKWWVHTRNVYISMSYLYGHRFSMPPNKLVQALRDELYDIPYQQINWPAQRTNVSAADRLTDPTWIQRSFTSALTMYETFKIPFLRRRALNEALFQIETETRNTHYLCIAPVSFASNMLALYHAHGRDSHWIRGMRDRFIDPMWLCREGLAASGTNGTSLWDTALTVQATIDAGLAARPENQAILRKALEFIDNSQIREDPLGVHHVYRQPTRGAWPFSTRDQSYAVSDTTAEAVKVIVLLQRIEGFPSRISDERLQQAIDLILGMENAGGGFSAYEPVRGPKFLELLNITELYENVMTDNLYPECTSSVIMCLTTFAREYPTYRPRDIQACLSRSIDYLLRSQYPNGGWFASWGVCFTYATMFALQGLACMGWNESNCAACQRACSFLLQHQNPDGGWGESLDTVRFKQYLPHPDGSQVTNTAYAVIGLLAARCGNHEAIRRGVAYLVKEQQDTGEWLPGPLEGVFAPPGGMRYPNYKFHFTLMALGRYVAIHGNECLAI