ID A0A218VS70_PUNGR Unreviewed; 670 AA.
AC A0A218VS70;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Acyl-CoA-binding domain-containing protein 4-like {ECO:0000313|RefSeq:XP_031404345.1};
GN Name=LOC116213507 {ECO:0000313|RefSeq:XP_031404345.1};
GN ORFNames=CDL15_Pgr020224 {ECO:0000313|EMBL:OWM62930.1};
OS Punica granatum (Pomegranate).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Lythraceae; Punica.
OX NCBI_TaxID=22663 {ECO:0000313|EMBL:OWM62930.1, ECO:0000313|Proteomes:UP000197138};
RN [1] {ECO:0000313|Proteomes:UP000197138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Dabenzi {ECO:0000313|Proteomes:UP000197138};
RX PubMed=28654223; DOI=10.1111/tpj.13625;
RA Qin G., Xu C., Ming R., Tang H., Guyot R., Kramer E.M., Hu Y., Yi X.,
RA Qi Y., Xu X., Gao Z., Pan H., Jian J., Tian Y., Yue Z., Xu Y.;
RT "The pomegranate (Punica granatum L.) genome and the genomics of
RT punicalagin biosynthesis.";
RL Plant J. 91:1108-1128(2017).
RN [2] {ECO:0000313|EMBL:OWM62930.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Fresh leaf {ECO:0000313|EMBL:OWM62930.1};
RA Xu C.;
RT "The pomegranate genome and the genomics of punicalagin biosynthesis.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:XP_031404345.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_031404345.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the ACBP family.
CC {ECO:0000256|ARBA:ARBA00005567}.
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DR EMBL; MTKT01006319; OWM62930.1; -; Genomic_DNA.
DR RefSeq; XP_031404345.1; XM_031548485.1.
DR OrthoDB; 52705at2759; -.
DR Proteomes; UP000197138; Unassembled WGS sequence.
DR Proteomes; UP000515151; Chromosome 7.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR InterPro; IPR000582; Acyl-CoA-binding_protein.
DR InterPro; IPR035984; Acyl-CoA-binding_sf.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR PANTHER; PTHR46093:SF3; ACYL-COA-BINDING DOMAIN-CONTAINING PROTEIN 4; 1.
DR PANTHER; PTHR46093; ACYL-COA-BINDING DOMAIN-CONTAINING PROTEIN 5; 1.
DR Pfam; PF00887; ACBP; 1.
DR Pfam; PF01344; Kelch_1; 1.
DR Pfam; PF13415; Kelch_3; 2.
DR SUPFAM; SSF47027; Acyl-CoA binding protein; 1.
DR SUPFAM; SSF117281; Kelch motif; 1.
DR PROSITE; PS51228; ACB_2; 1.
PE 3: Inferred from homology;
KW Kelch repeat {ECO:0000256|ARBA:ARBA00022441};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 12..103
FT /note="ACB"
FT /evidence="ECO:0000259|PROSITE:PS51228"
FT REGION 640..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 670 AA; 73312 MW; BEC21BDC81DB4E38 CRC64;
MVMARASSGP AYPDRFYAAA SYAGFGESPQ GVASRFPNDI ALLLYALYQQ ATKGPCNVPK
PRGWSPVEQS KWTSWHGLGN MASAEAMRLF VKILEEEDPS WFSRASAIAD PVVDVDTNHT
FKSEPVIENG ESDAQTKIVS SENGILNETQ DKDVVSEGLS SIAVYDQWVA PSVQGPRPKA
RYEHGAAVIR DKMYVYAGNH NGRYLNDMHI LDLRSWTWSK VEAKFNDDTA ETSGSFAPCA
GHSLIPWNNK LLSVAGHTKD PSETMQVREF DPQTATWSIL KTYGKAPVSR GGHSVTLVGN
TLVIFGGQDA RRSLLNDLHI LDLETMTWDE FDALGTPPSP RSDHSAAVHA ERYLLIFGGG
SHATCFNDLH VLDIQTMEWS RPTQQGEIPT SRAGHAGATV GENWFIVGGG DNKSGASETI
MLNMSTLVWS IVTAVQGRVP VVSEGLSLVV SSYNGEDVLV SFGGYNGRYN NEIHVLKPSH
KSTIPSKMTE SSLPDSTSAV HNVTHAPRDV ELEVEAVQDG RIREIAVDNA LNPTKSKGQA
NGEPLLTTIK AEKEELESLL SKEKVLSLQL KEDLLEAEAR NANLYKELQS LRGQLAAEQS
RSFKLEVDVA ELRQKLQTME ALQKELEILR RQKAASEQAI SMARQKQSSG GVWSWLTGTP
PSPGEKENNA
//
