ID A0A443N5S7_9MAGN Unreviewed; 669 AA.
AC A0A443N5S7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Putative DUF21 domain-containing protein, chloroplastic isoform X1 {ECO:0000313|EMBL:RWR73868.1};
GN ORFNames=CKAN_00217500 {ECO:0000313|EMBL:RWR73868.1};
OS Cinnamomum micranthum f. kanehirae.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Laurales; Lauraceae; Cinnamomum.
OX NCBI_TaxID=337451 {ECO:0000313|EMBL:RWR73868.1, ECO:0000313|Proteomes:UP000283530};
RN [1] {ECO:0000313|EMBL:RWR73868.1, ECO:0000313|Proteomes:UP000283530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chaw 1501 {ECO:0000313|Proteomes:UP000283530};
RC TISSUE=Young leaves {ECO:0000313|EMBL:RWR73868.1};
RX PubMed=30626928; DOI=10.1038/s41477-018-0337-0;
RA Chaw S.M., Liu Y.C., Wu Y.W., Wang H.Y., Lin C.I., Wu C.S., Ke H.M.,
RA Chang L.Y., Hsu C.Y., Yang H.T., Sudianto E., Hsu M.H., Wu K.P., Wang L.N.,
RA Leebens-Mack J.H., Tsai I.J.;
RT "Stout camphor tree genome fills gaps in understanding of flowering plant
RT genome evolution.";
RL Nat. Plants 5:63-73(2019).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:RWR73868.1}.
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DR EMBL; QPKB01000001; RWR73868.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443N5S7; -.
DR STRING; 337451.A0A443N5S7; -.
DR Proteomes; UP000283530; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR CDD; cd04590; CBS_pair_CorC_HlyC_assoc; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR002550; CNNM.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR044751; Ion_transp-like_CBS.
DR InterPro; IPR005170; Transptr-assoc_dom.
DR PANTHER; PTHR22777; HEMOLYSIN-RELATED; 1.
DR PANTHER; PTHR22777:SF17; UPF0053 INNER MEMBRANE PROTEIN YFJD; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF01595; CNNM; 1.
DR Pfam; PF03471; CorC_HlyC; 1.
DR SMART; SM00116; CBS; 2.
DR SMART; SM01091; CorC_HlyC; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS51846; CNNM; 1.
PE 4: Predicted;
KW CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW ProRule:PRU00703};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU01193}; Reference proteome {ECO:0000313|Proteomes:UP000283530};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU01193};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|PROSITE-
KW ProRule:PRU01193}.
FT TRANSMEM 102..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 241..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 280..302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 151..337
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000259|PROSITE:PS51846"
FT DOMAIN 356..417
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 424..481
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 633..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..660
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 669 AA; 74527 MW; 9EFA05C31F532EAC CRC64;
MDFAVLEASI LGRTTFIALP KPPVLIKINS CCRISGRFRP RTPLLSLRVA KNCGGVGRAD
FSSHRDLDVL RGWVVSGGRE VGRGSIEESD FEVFRVFARR GLLLALVVCG VFLIGGCRRV
LAMEGILDAG VRVFEKGGVL FKGAWPKMLL VLKVLREQGL VLTALLGLSA FFSMAETSIT
TLWPWKVREL AEKEPENGVF KMLRSDVTRF LTTILIGTTV VNIVATALVT EAATATFGEA
GVSAATGVMT VAILLLTEIT PKSIAVHYAT DVVRFVVRPV AWLSFILYPV GRVATFLSMG
MLKILGLKGR SEPYVTEDEL KLMLRGAELS GAIEEEEQDM IENVLEIKDT HVREVMTPLV
DVVAIDASAT LNDFQKFWVI HQYSRVPVFE ERVDNIVGIV YAMDMLEFVE KVDQLESSTV
GEIAHKPAFF VPDSMSVWNL LREFRNRKVH MAIVLNEYGG AIGIVTLEDV VEEIVGEIFD
ENDSKEEIQK KTGYIVMRAD GTYDVDANTS IDQLSEDLNI EMPEGQQYET VSGFVCESFG
YIPRSGESIK VVLKDANREE NSEYSETGSD HQDQMEKNQI YKLVILEGNA RKVKSVRFER
INQDDTKLKT KAVARVIPKI MKRKWRGADY LERPDHEGLR RTSGDSFSDS HIEEHGGGGP
DNNNEQELQ
//
