ID A0A364L550_9EURO Unreviewed; 1968 AA.
AC A0A364L550;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN ORFNames=BHQ10_006959 {ECO:0000313|EMBL:RAO70947.1};
OS Talaromyces amestolkiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO70947.1, ECO:0000313|Proteomes:UP000249363};
RN [1] {ECO:0000313|EMBL:RAO70947.1, ECO:0000313|Proteomes:UP000249363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIB {ECO:0000313|EMBL:RAO70947.1,
RC ECO:0000313|Proteomes:UP000249363};
RX PubMed=28649280; DOI=10.1186/s13068-017-0844-7;
RA de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L.,
RA Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.;
RT "Differential ?-glucosidase expression as a function of carbon source
RT availability in Talaromyces amestolkiae: a genomic and proteomic
RT approach.";
RL Biotechnol. Biofuels 10:161-161(2017).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RAO70947.1}.
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DR EMBL; MIKG01000013; RAO70947.1; -; Genomic_DNA.
DR STRING; 1196081.A0A364L550; -.
DR OrthoDB; 2330615at2759; -.
DR Proteomes; UP000249363; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.2450; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 7.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR24189; MYOTROPHIN; 1.
DR PANTHER; PTHR24189:SF50; MYOTROPHIN-RELATED; 1.
DR Pfam; PF12796; Ank_2; 5.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 19.
DR SUPFAM; SSF48403; Ankyrin repeat; 4.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 9.
DR PROSITE; PS50088; ANK_REPEAT; 10.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000249363};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 12..273
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT REPEAT 950..982
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 983..1015
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1016..1048
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1215..1243
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1318..1350
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1440..1465
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1649..1681
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1766..1798
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1799..1831
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1853..1881
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
SQ SEQUENCE 1968 AA; 218904 MW; F246A14EDB7D3DBE CRC64;
MGHAIPNGIL QSQPKLEHAL RCLVEKSEYC TLRTGSEVID REELATHMVV TYLDHRSKTK
KHLRAQWLIG ADGKRGVVRK KFLEPTAGIK QEDGIFRYEG TWIAANLHMT LPTPATHPDL
DVLWDLGLTA EEVYDLFWPK GWHFCAPPGK PTACGRFGPH EDRLWRHEFA EPDWSDDGSK
NAEELFWEHL TPMITLSADA TGRQFGREIT FPKDCIEIMR CRPFKFTHKV VNRWFDNRTI
LIGDAAHVFP PFGGQGIACG IRDAEELSWR IAILASLKSS IPQGVINGVL SAWAKERHLG
VENSMRHTMI SGNLCNGTAG LAYTALAPLL LPLLTLPSFR GFPTPLSHGE VTGYRSVKDG
FFLSKYGGGY KLAQTYAIAT FPTNSLPESS LRWEMVLSDQ ILYHVPTPFI LLIAGQLLAE
EKSQVQKLLR STRLESTILS DQSIIQLHKS QKDLETSLKR EITNRPKSPR HGLADQQSFY
GAMVRPEWEK AISLVIDHLL EERRKNSLVV YFFCDFSSQN QVNIINILHH ILRQVIIQGS
GEMLSMLKES CGDPSTLQNE TRVVQLLALA ASVQPIYMVI DGLDELKTPN ELLAQIPELA
KSEIHILITS RDLPQIRKKM GPAIHLAIKP TDSDLRLYVA SRLQGSEFAE EVARDSSLVN
EIVSKTGNMC VITFPSGVPT LTERRFLLSR FLLDELLDLV TIHQIRKALQ RPPRGLEQAL
EATLQRIDAQ PPARTTLARR LLGWIMVAER RLKLDEVITA FAVEDGQELQ RDNMPSPDIL
LQVCAGLVVL NEHDNTLGLV HAFAYEVLHL SLPQKEANLD MAXTCLRYLS LKPLATGSCA
SSTEMIKRLN SLAFLDYSSK HWGQHVVLGN FETELETLIM KLLDDTALRN SAFQALQFRG
DFANSGVTEE LFESMPTNPE ALHLAAYWGL TYIAGKYLEA GAPPSAIDSH RWTPLHWACA
NDKLPVAKVL ILSGADVNAQ DIQGWSPLFW AAFVGNTDTV RLLLSSGANH LARSEFGWTA
LHWAVSGGHT AIVKELLEYX SQLQSSEPVF HKMTMEEIES YANATLPVDV AAAGQDSNIF
TMLIEHLQTP PDIVTDVKFN MIWERERFDV PVSHNPWRTL TKGERVNGRE SNIPRFTGRF
ARSSEEWRSD SKKWKSVLLL SAIRDQQLSS VELLVETGAD VDYKNALCVA ACRRDPRYVQ
CLLKNGANPN IEDRYGRTAL HEAVMNGFVE TIAALLDGGA DINKPVARNY HMSDSDDPIS
LPGYRIKLSE NGSTALIQAS GFSLNTFLIA EPSDSDLAMQ ITRLLLSRGA DPCLKDGSGR
TALHYAVLRP HLPLVEILVE AGCPTDAVDH NGATPMHLLA FHRKEFLNLH YLKKVVSLLI
KGKYENGRTK ILDQSVCAKP AHGAEPEGEG GDKSVLYKET VIKETRGQYI KLKRLEGFVE
GLTPLSMALQ AGRWGLVQVL LELGATFPVD LNLTPILDHA IKSVEPNMTN LLLQHRAHPS
PDAIYSLCIS FVAQTTSTEP LEGRDIDADF GAVLEKLVSA GADINFCQDE ETPLTLVANK
RGSQFALKAL IDAGADIYKV SSKTFDPILT VALFREAGDL AYLLDYAVAH PKEDHWSRHL
TEFPNESDPI MRICLCLQKV DGMNDTNNDG RTLLHFAAEK GHITLVTSLV SCGAKADIAD
SKQWLAIHCA GFAQQTAVMK FLLEHSTDSS VKMQEIFEED NTSLKHTMLD VAIIKQNIDM
VRVILKYGSK VHPSIDINSK IRNWRRDVPM LGYAAENGYE DILSILLQNG ADIEGTDKYG
WRPLHFACYR GHTEIAKILI DAGADVHAAT GKWNEANIKP TGLYQDDNWT GQPLHLATMS
GQADIVKLLL EKGVDIHAST GVDPESSYHW PGHGPTALHL ALDTNLFYGR RGQALDAGRL
QIAQWLVERG AMVRGIIGRY SLQDILNFRD SPGLWDALVA GERDEASI
//