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Database: UniProt
Entry: F0Y9K2_AURAN
LinkDB: F0Y9K2_AURAN
Original site: F0Y9K2_AURAN 
ID   F0Y9K2_AURAN            Unreviewed;      1795 AA.
AC   F0Y9K2;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AURANDRAFT_71657 {ECO:0000313|EMBL:EGB08328.1};
OS   Aureococcus anophagefferens (Harmful bloom alga).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Pelagophyceae; Pelagomonadales;
OC   Aureococcus.
OX   NCBI_TaxID=44056 {ECO:0000313|Proteomes:UP000002729};
RN   [1] {ECO:0000313|EMBL:EGB08328.1, ECO:0000313|Proteomes:UP000002729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP 1984 {ECO:0000313|Proteomes:UP000002729};
RX   PubMed=21368207; DOI=10.1073/pnas.1016106108;
RA   Gobler C.J., Berry D.L., Dyhrman S.T., Wilhelm S.W., Salamov A.,
RA   Lobanov A.V., Zhang Y., Collier J.L., Wurch L.L., Kustka A.B., Dill B.D.,
RA   Shah M., VerBerkmoes N.C., Kuo A., Terry A., Pangilinan J., Lindquist E.A.,
RA   Lucas S., Paulsen I.T., Hattenrath-Lehmann T.K., Talmage S.C., Walker E.A.,
RA   Koch F., Burson A.M., Marcoval M.A., Tang Y.Z., Lecleir G.R., Coyne K.J.,
RA   Berg G.M., Bertrand E.M., Saito M.A., Gladyshev V.N., Grigoriev I.V.;
RT   "Niche of harmful alga Aureococcus anophagefferens revealed through
RT   ecogenomics.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:4352-4357(2011).
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DR   EMBL; GL833128; EGB08328.1; -; Genomic_DNA.
DR   RefSeq; XP_009037051.1; XM_009038803.1.
DR   EnsemblProtists; EGB08328; EGB08328; AURANDRAFT_71657.
DR   GeneID; 20228327; -.
DR   KEGG; aaf:AURANDRAFT_71657; -.
DR   eggNOG; KOG0430; Eukaryota.
DR   InParanoid; F0Y9K2; -.
DR   OMA; PVTQCAG; -.
DR   OrthoDB; 3715804at2759; -.
DR   Proteomes; UP000002729; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.790; -; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 1.
DR   Gene3D; 3.30.365.10; Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain; 4.
DR   Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR   Gene3D; 1.20.120.1740; Sodium ion translocating NADH-quinone reductase subunit C-like; 1.
DR   InterPro; IPR002888; 2Fe-2S-bd.
DR   InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR   InterPro; IPR016208; Ald_Oxase/xanthine_DH-like.
DR   InterPro; IPR008274; AldOxase/xan_DH_MoCoBD1.
DR   InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2.
DR   InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR005107; CO_DH_flav_C.
DR   InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR008978; HSP20-like_chaperone.
DR   InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR   InterPro; IPR040933; PSII_Pbs31.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR11908:SF132; ALDEHYDE OXIDASE 1-RELATED; 1.
DR   PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR   Pfam; PF03450; CO_deh_flav_C; 1.
DR   Pfam; PF00941; FAD_binding_5; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF01799; Fer2_2; 1.
DR   Pfam; PF02738; MoCoBD_1; 1.
DR   Pfam; PF20256; MoCoBD_2; 1.
DR   Pfam; PF18240; PSII_Pbs31; 1.
DR   SMART; SM01092; CO_deh_flav_C; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR   SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 1.
DR   SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR   SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   4: Predicted;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Iron {ECO:0000256|ARBA:ARBA00022714};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002729}.
FT   DOMAIN          213..291
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          396..593
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   REGION          1591..1615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1773..1795
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1795 AA;  187419 MW;  EA9C460058351485 CRC64;
     MKLSFLLFGG AAALAPQPVK LDRRQAMKTV AGTFAAAVAA PQIASADGAV SAATVARSRG
     IYGGRIADLK DAVEKGDFAA VLAEKNAFDL FNSGAYAQKS AITKAQKAIA VTETKNIMEA
     IASKNANQLK TSYAAYMKNA AIDTKPVDVS TGQGYSNDYD WKRAFPASTP MYLYLLALVV
     LSWVLLRLRR RAEPVEARSE DPVKSPPAED PPSTVVLTIN GAVHCVENPS PSLTLLAYLR
     DRCGLTAAKV GCGEGGCGAC TVVEHNTDAI NACLRLLCQC DGSVITTAEG LGSSRNGFGD
     IQKAIADGNG SQCGYCTPGW TTAVAALRAR GPRSRGDLQK KLDGNICRCT GYRPILEALE
     GLPDVEDAAP CRDVTTGRAC GRACGAPPSR GLSVADDARR LSYVEPTSLP RLYALLDAGL
     GYGETVLVGG ATAAIGVAKY YDDCLGAPWA GGLPPLEDAQ LVATKSVPEL TKLAAADDGL
     AAGGAVTIDA LSAALRGGLD VAWNAAAAHL DRVANTQVRN SATWAGNLAL AARADGFPSD
     VAVALACLGA ELSVSRRDGK TKRRLQKLAV VDVLTGWRAG DVVVELFVPR SPAGTTARCD
     KVAARHANAH AYVNAGLSVR VASGVVASAR LFFGGVAPRT KLFRATAAEA ALAGKPVADA
     DAFQAAVAAL RAQLPTDDAY ATDCAVQLLY KACLLAQPSL PPRVANALRS LAAHRPPSSG
     ARDVAGASDG RYAPACAPRV KLAARLQASG EARYAADEPR ACNEVSVAFA FAKRSGTVTA
     VDVSGAARVL GAVAVYSRDD ALRDLVATES LALDDADDLL LWGVGDDVFV GCRVALCVGT
     SDLAALAMAR AVRCATDGGA GGAAALTSAE LKAALAAHFS DDGSGKGRKL GLRRGALRVV
     DDHVVLKTTS STTTDDRVVL KTTSSTKTDD RVVLKTTSST KTVSGAFATP LQKHFHMETH
     SARCVPGEGS RLLLTASTQD PTLTQTVTAS LLGLRAADVV VACRRAGGGF GGKLTLHLPA
     ATSVALVAAK LGVPARYHAD RRDDMAMTGG REATACDYEV SFDAATGALA SYAATFAVEG
     GHATQDAVGD LSMAVQWSDN CYDSGRHDAK GKVLKTRAPR SSSMRSPGVI QSQCCRELAI
     VRVAHETRRP VHEVQELNFY KVGQKFPYGS KPLGSPTFNY TIPELYAALK PKLLARLDAV
     DQFNEANAWR KRGVHVMPTK YIMAMDFWKV PALVNVYGDG SVQVAHGGCE LGQGIHTKVA
     AVAAYALGCD LSLVTVADTS TDKTPNSVAT GGSGTSESCC GATLKACATL KKRLAPYVAK
     HAKWADAVAA ALADAVELSA TGWNDLRTSE SGDDPDYATY GLALAEVEVD CLSGEVEVRE
     VDVRMDQGSS LNSDVDVGQV EGAIVMALGF YLTEHCAVDA SGKQSGDGTW EYKPPMVADV
     PLDLRVSMLA RTPNPSAVAV LGSKASGEPP MQLAASVFFA LRAAVAAFRR DALGDAAWFD
     LPVPASPKAI RAALGRLDDA GLVFAYSMAT DDRFDSLSFC AFHFEMWGRT GDAARVPSPS
     RALSTNRTAR ATAETESMAA LAAMAGKLGL DMDDLNDSDR PPPGPPKDPN EPVLAPVMGK
     SSVEVIEGSD EIRPEGWWHP KGASEQGQKS DAPVLAPEKL AAEAASAYVE TVPFDTFALS
     DEGKKVVLYF GLPGAKANLG KDAVAASFRT QALEVTARVG SKRYRFHESI IYEHIVPAKG
     KVKVKSDHVV VTMFKVHAAC PWDTISVNRK AVGPVRTSPP DHGRPTVVTA SGDAA
//
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