GenomeNet

Database: UniProt
Entry: A0A2V3IC68_9FLOR
LinkDB: A0A2V3IC68_9FLOR
Original site: A0A2V3IC68_9FLOR 
ID   A0A2V3IC68_9FLOR        Unreviewed;       310 AA.
AC   A0A2V3IC68;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   SubName: Full=Acyl-CoA-binding domain-containing protein 1 {ECO:0000313|EMBL:PXF39702.1};
GN   ORFNames=BWQ96_10602 {ECO:0000313|EMBL:PXF39702.1};
OS   Gracilariopsis chorda.
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gracilariales;
OC   Gracilariaceae; Gracilariopsis.
OX   NCBI_TaxID=448386 {ECO:0000313|EMBL:PXF39702.1, ECO:0000313|Proteomes:UP000247409};
RN   [1] {ECO:0000313|EMBL:PXF39702.1, ECO:0000313|Proteomes:UP000247409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SKKU-2015 {ECO:0000313|EMBL:PXF39702.1,
RC   ECO:0000313|Proteomes:UP000247409};
RC   TISSUE=Whole body {ECO:0000313|EMBL:PXF39702.1};
RX   PubMed=29688518; DOI=10.1093/molbev/msy081;
RA   Lee J., Yang E.C., Graf L., Yang J.H., Qiu H., Zel Zion U., Chan C.X.,
RA   Stephens T.G., Weber A.P.M., Boo G.H., Boo S.M., Kim K.M., Shin Y.,
RA   Jung M., Lee S.J., Yim H.S., Lee J.H., Bhattacharya D., Yoon H.S.;
RT   "Analysis of the draft genome of the red seaweed Gracilariopsis chorda
RT   provides insights into genome size evolution in Rhodophyta.";
RL   Mol. Biol. Evol. 0:0-0(2018).
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:PXF39702.1}.
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DR   EMBL; NBIV01000506; PXF39702.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V3IC68; -.
DR   STRING; 448386.A0A2V3IC68; -.
DR   Proteomes; UP000247409; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   InterPro; IPR000582; Acyl-CoA-binding_protein.
DR   InterPro; IPR035984; Acyl-CoA-binding_sf.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   PANTHER; PTHR24119; ACYL-COA-BINDING DOMAIN-CONTAINING PROTEIN 6; 1.
DR   PANTHER; PTHR24119:SF0; ACYL-COA-BINDING DOMAIN-CONTAINING PROTEIN 6; 1.
DR   Pfam; PF00887; ACBP; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   PRINTS; PR00689; ACOABINDINGP.
DR   SMART; SM00248; ANK; 3.
DR   SUPFAM; SSF47027; Acyl-CoA binding protein; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   PROSITE; PS51228; ACB_2; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 2.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247409};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        291..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          22..109
FT                   /note="ACB"
FT                   /evidence="ECO:0000259|PROSITE:PS51228"
FT   REPEAT          173..205
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          206..238
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
SQ   SEQUENCE   310 AA;  34117 MW;  3706EFA36C612BB7 CRC64;
     MLHTCSVSDV RSNSASAMTT AIVSSFEDAA DFVSSGKLGS ISQDEQLELY GLYSVVRKGS
     APNKAPSALL DPTGFAKWTA WQTYSHLEKE DAMKEYIELV SSLLASSRPK TSSSTQSTGF
     GNKGSGGFDI QADNEELSNN ELDICYYATM GDKASVIRCL KKQRVSPNYR DQDGLTPLMR
     AVDRNEMHVV DILVAAGADL NAVDDEGQTA LHYAVCCDYS EMTALLLYHG ARTDIVDKHG
     DGALGIASDE TKRAIEEVQQ GTWKRKSPQF NVGRWWFSYF SPVHFEFNTQ VLAASAFITV
     GIILYYHLRQ
//
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