ID   E1ZKZ0_CHLVA            Unreviewed;      1020 AA.
AC   E1ZKZ0;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   ORFNames=CHLNCDRAFT_136738 {ECO:0000313|EMBL:EFN53465.1};
OS   Chlorella variabilis (Green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX   NCBI_TaxID=554065 {ECO:0000313|Proteomes:UP000008141};
RN   [1] {ECO:0000313|EMBL:EFN53465.1, ECO:0000313|Proteomes:UP000008141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NC64A {ECO:0000313|EMBL:EFN53465.1,
RC   ECO:0000313|Proteomes:UP000008141};
RX   PubMed=20852019; DOI=10.1105/tpc.110.076406;
RA   Blanc G., Duncan G., Agarkova I., Borodovsky M., Gurnon J., Kuo A.,
RA   Lindquist E., Lucas S., Pangilinan J., Polle J., Salamov A., Terry A.,
RA   Yamada T., Dunigan D.D., Grigoriev I.V., Claverie J.M., Van Etten J.L.;
RT   "The Chlorella variabilis NC64A genome reveals adaptation to
RT   photosymbiosis, coevolution with viruses, and cryptic sex.";
RL   Plant Cell 22:2943-2955(2010).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
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DR   EMBL; GL433851; EFN53465.1; -; Genomic_DNA.
DR   RefSeq; XP_005845567.1; XM_005845505.1.
DR   AlphaFoldDB; E1ZKZ0; -.
DR   STRING; 554065.E1ZKZ0; -.
DR   GeneID; 17352977; -.
DR   KEGG; cvr:CHLNCDRAFT_136738; -.
DR   eggNOG; ENOG502QVGN; Eukaryota.
DR   InParanoid; E1ZKZ0; -.
DR   OrthoDB; 455805at2759; -.
DR   Proteomes; UP000008141; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.40.462.20; -; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 2.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR006093; Oxy_OxRdtase_FAD_BS.
DR   PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR   PANTHER; PTHR42973:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
DR   PROSITE; PS00862; OX2_COVAL_FAD; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008141};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        9..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        47..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        207..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        245..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          598..772
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   1020 AA;  110045 MW;  406A6C5A7267330D CRC64;
     MSGLFGDLLL IRLCLTMAYI WLMTAASVGY PAWPGVSNPG FYSLDGIIWA TLNLFFHGCA
     LFQLFWDERR ITFKDADLHQ LWQFLYRRSG MGKLEVLEST KRARFVRFKA GEEILSAAAT
     KCTLMLLVEG LATYRMEDDK GNTLKDDTQL ISGQTFDIGL LNVLGTADVV AAVKFATSHG
     LQLAARSGGH GAGSASFLMS GLFGDLLLIR LCLTMAYIWL MTAASVGYPA WPGVSNPGFY
     SLDGIIWATL NLFFHGCALF QLFWDERRIT FKDADLHQLW QFLYRRSGMG KLEVLESTKR
     ARFVRFKAGE EILSAAATKC TLMLLVEGLA TYRMEDDKGN TLKDDTQLIS GQTFDIGLLN
     VLGVYIAFEH GEGERRLVRA VSDCTVVLWD LDYLNYLATR CSPAVSAFWR NFALCQTGLE
     WFHRAHLGQP PVNGRGHPEP AGITQGLARS SDFTDPLEPY EDPSPTLKGV LTWLPSTLAP
     FLPSGMRHTA MPRAGALARN RLMALGGSGR GNLDAVLSQE PLELRYTSQK IVNAISAELS
     SSAPGSRAGS KAMCNIMDGV EALRASVRGN VLLPADEGFA EAIKVWGVSP SHTLNGQTAP
     TPALVIQPRG TADVVAAVKF ATSHGLQLAA RSGGHGAGNP SWVDGGLMVD MSLMGRWVIV
     YVDPAEKTAV VDGGALACYI DADTALHGLA VPLGVCAVVG VGGLALHGGL SVLSRAHGAT
     CDSLLEAQLV LADGSVVHAT KDGPDPELLW ALKGAGSLFG IVTKVKLQLY EAPTYSGAMV
     WKDDPEHVNY KAILRWIRST VLPNPCLGFN CGRMLDPELG PVLVSMVVVT GEQPDTVGQS
     TWLQTQMTHY EGVTGLTEAY PGHFEAATGG HVKAEHFTDE FIDTYVRCAT EELPLPDLGL
     TLSFIELMGG ALKDSTSPIG LKEGDLQWVV QAGWSDAAAN PVGLRYTGML REVLGPLSTS
     MSQYVNLLDV AEDLDMSYES AAAKAGGAAN LEKIRALKAK YDPTGVFLNS PYTKVLAVKP
//