ID F4W6W6_ACREC Unreviewed; 498 AA.
AC F4W6W6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Protein TMED8 {ECO:0000313|EMBL:EGI70079.1};
GN ORFNames=G5I_01172 {ECO:0000313|EMBL:EGI70079.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI70079.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GL887762; EGI70079.1; -; Genomic_DNA.
DR RefSeq; XP_011064658.1; XM_011066356.1.
DR AlphaFoldDB; F4W6W6; -.
DR STRING; 103372.F4W6W6; -.
DR EnsemblMetazoa; XM_011066356.1; XP_011064658.1; LOC105152215.
DR GeneID; 105152215; -.
DR KEGG; aec:105152215; -.
DR eggNOG; KOG3878; Eukaryota.
DR InParanoid; F4W6W6; -.
DR OrthoDB; 2909903at2759; -.
DR Proteomes; UP000007755; Unassembled WGS sequence.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.60.120.680; GOLD domain; 1.
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; IPR009038; GOLD_dom.
DR InterPro; IPR036598; GOLD_dom_sf.
DR PANTHER; PTHR22973; LD35087P; 1.
DR PANTHER; PTHR22973:SF12; LD35087P; 1.
DR Pfam; PF00887; ACBP; 1.
DR Pfam; PF13897; GOLD_2; 1.
DR SUPFAM; SSF47027; Acyl-CoA binding protein; 1.
DR SUPFAM; SSF101576; Supernatant protein factor (SPF), C-terminal domain; 1.
DR PROSITE; PS51228; ACB_2; 1.
DR PROSITE; PS50866; GOLD; 1.
PE 4: Predicted;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Reference proteome {ECO:0000313|Proteomes:UP000007755}.
FT DOMAIN 59..150
FT /note="ACB"
FT /evidence="ECO:0000259|PROSITE:PS51228"
FT DOMAIN 336..488
FT /note="GOLD"
FT /evidence="ECO:0000259|PROSITE:PS50866"
FT REGION 162..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..318
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..416
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 498 AA; 58520 MW; C025F20F9D9F5DB2 CRC64;
MLTQMAAAVE EDVSTLSEWV DELSVSATED DKNATSRTDS NDVDVTAKNC EPRLWGFETR
ELYKFALNFY KEKEGKAVHL SYEDKLKLVA FTQQVTHGKY TAENAPSLGV LDMIGRDRRV
AWQNLGDISK EQAMEGFIIL LDKLCPLFRT VVEAQKRNFE EKQRLKREEE AKKQEEEKKL
KELEEEKKKQ EEERLKEETQ RRQIQDALNQ QTYYQFRLYA EQQYPGNPEQ QGVLIRQLQE
QHYHQYMQQL HQNQLVVEDH IEEEEEEEKE KKMKKKDIQN QSKNVTCKDN DDHDDDDDDK
DNTNENVNDE DSDEVEDWPP INPAEMWTRK GVEEFKQIIR KETGDAVIKV GHGETVTVRV
PTHEDGTCLF WEFATDGYDI GFGVYFEWSK PETNQVSVYI SESEEDEDEE EYESREDLES
GSVNGNARPE RKTTTPPISV IVPIYRRDSQ EEIYAGSHQY PGEGVYLLKF DNSYSLWRSK
TLYYRVYYTR QGFTKNNN
//
