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Database: UniProt
Entry: A9VAS6_MONBE
LinkDB: A9VAS6_MONBE
Original site: A9VAS6_MONBE 
ID   A9VAS6_MONBE            Unreviewed;      1658 AA.
AC   A9VAS6;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDQ85372.1};
GN   ORFNames=MONBRDRAFT_29328 {ECO:0000313|EMBL:EDQ85372.1};
OS   Monosiga brevicollis (Choanoflagellate).
OC   Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Monosiga.
OX   NCBI_TaxID=81824 {ECO:0000313|EMBL:EDQ85372.1, ECO:0000313|Proteomes:UP000001357};
RN   [1] {ECO:0000313|EMBL:EDQ85372.1, ECO:0000313|Proteomes:UP000001357}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MX1 / ATCC 50154 {ECO:0000313|Proteomes:UP000001357};
RX   PubMed=18273011; DOI=10.1038/nature06617;
RG   JGI Sequencing;
RA   King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J.,
RA   Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D.,
RA   Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M.,
RA   Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S.,
RA   Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T.,
RA   McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.;
RT   "The genome of the choanoflagellate Monosiga brevicollis and the origin of
RT   metazoans.";
RL   Nature 451:783-788(2008).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the SAPS family.
CC       {ECO:0000256|ARBA:ARBA00006180}.
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DR   EMBL; CH991574; EDQ85372.1; -; Genomic_DNA.
DR   RefSeq; XP_001749783.1; XM_001749731.1.
DR   STRING; 81824.A9VAS6; -.
DR   EnsemblProtists; EDQ85372; EDQ85372; MONBRDRAFT_29328.
DR   GeneID; 5895030; -.
DR   KEGG; mbr:MONBRDRAFT_29328; -.
DR   eggNOG; KOG1469; Eukaryota.
DR   eggNOG; KOG2073; Eukaryota.
DR   InParanoid; A9VAS6; -.
DR   Proteomes; UP000001357; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0019903; F:protein phosphatase binding; IEA:InterPro.
DR   GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IBA:GO_Central.
DR   CDD; cd05154; ACAD10_11_N-like; 1.
DR   Gene3D; 3.90.1200.10; -; 1.
DR   Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR   Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR   Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR   InterPro; IPR041726; ACAD10_11_N.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   InterPro; IPR002575; Aminoglycoside_PTrfase.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR007587; SAPS.
DR   PANTHER; PTHR48083:SF13; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR   PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF01636; APH; 1.
DR   Pfam; PF04499; SAPS; 2.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001357}.
FT   DOMAIN          959..1176
FT                   /note="Aminoglycoside phosphotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF01636"
FT   DOMAIN          1373..1475
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          1487..1636
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   REGION          654..759
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          838..890
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        671..685
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        698..716
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        741..759
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        846..863
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        876..890
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1658 AA;  181695 MW;  12A67957779B4644 CRC64;
     MFWEFDFNST SQIDKILDEE TCTLEQILDQ DDVLQECKAS NDKLLKYLTV EAQLDRLIRY
     VVDMPDDPDE MNRFKYSSIA SEVLTCDAWS MTSAVSEAPV LNRFYAYFEQ DEVLHPLHAS
     FVVRVLSGLF QKSNESMAAH LKENPQHLRS IIKHIRTPAV VELLVCISGS EMNLQDWLTS
     NEHHFVEDIL SKLAPAEQQD AEELSNVHRY ISEVVINCRR EASDQWQRAG DSPPSPLLAF
     LLRQDTVEQI LKDCFEGTSL SLEYSLEVLL ELVREPPIVD DDQEFSSIDR ARHKQEVQGV
     LAVLAPKFSQ LHDIVVTHKR EEPLQTGSGV LEKPVGKLRL TAVHLVVALM EFRHHDMIEE
     IIKAGTVGVC LAFLGDYPEN NFMHKYIFDM LSLAIPDPDN AAAGRKDEDD DSELVPTDDD
     PAAAEAVNDL YRHVFVDYNL FQRLLDLWAE NNRVQSEGKG HRLGYMGYWL KIADRILALE
     GSPRDPLTLF GDSDVVAGVA SSWRALVDQH IRPLLKVAKE PLGGAPPQGF ADSDDSDFYV
     PRSAEDYMRV AGTGDVSDNA ADNSAAFQDF CTAELAPKFP DFRPAAHGTE ESEEDIALNY
     GMDGIFSPGL VYDTDLAPFV VDGISSVQEP AYDEPAPDAL DTSMSVPIVN EAVASSTNDS
     GDASAPAAAD LDSSASESES GVRTPSAVAT GGGLPLSDSS EDEDEDEEDM ADADVDEEAG
     WTVKSVPMDG LARGASNEPV DEDEGDNSED KELDTDSDEE LSASYDLQTM SMTPTKPAID
     IPLSPRSTNA VRHIHTRADP QASSPVAASA SDELKTFALL EQDSSTDDLS KPAAIAADDA
     AGTAASPATA KSNGSNSSTP GSGVKKPERK RSLPSTPVPK NANLPSTIHT LPLSPSLSPL
     SPSLSLSPSL SPLSLSLSTT KFFVKERERE REREIFMIVK HGERDRGGWL PAVKGGGVTV
     RQFNNGQSNP TFWLAWPDQG PQLVVRKKPP GILLPKAHQV EREYAVLRAL YQQGFPVPEP
     LLLSDDDRVI GTPFYVMRYV QGRIFRDPEL KSLPEPQRRL YYDAVVATLN LDVAQMDLPD
     TMRKRGSYFG RQRHVWFKQY QLACTVVPPL PALEQLNTQL EAAAKQHTTD EQTCLTHGDF
     RIDNVIFHPT EPRVIAVLDW ELCAIGHPLA DLTYFCLPFH LDSITIGDVE LPGLRASTVA
     GLPTEGDVRM QYGSAAVNPQ TWAQYLGLGC LRLASIAQGV FARSRQGNAS AANASELRKV
     AERLAEVGLH VMTQGQAHGD QAPKHATQLP PALRLVQLSS KAAKLRETLL RFMEEELEYA
     ALAEITGRSL LAAEACNCSA PDTGNMEVLH LYGTPAQQEQ WLKPLLAGEI RSCFCMTEPD
     VASSDATNMA CSISRDGDGY RINGRKWWAT GAGDPRCRLA IVMGQTPDPQ RPKHQQHSMI
     LVPMDTPGVR KIRPLTHFGY DDAPHGHFEV VFDNVRVPAS NILLGEGRGF EIAQGRLGPG
     RLHHCMRAIG MAERAFELML GRALTRQTFG RPLARHGMIQ EYVALSRMEI DASRLLVLQA
     AHVIDQDGNK AARTHVATAK VTVARMAQAV LDRAIQVHGG AGVSADLPLA LMYAGARTLR
     IADGPDEVHL VSIAAAELRR FAKAHGVTAA QLSGASKL
//
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