ID A0A158P361_ATTCE Unreviewed; 353 AA.
AC A0A158P361;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=ACB domain-containing protein {ECO:0000259|PROSITE:PS51228};
GN Name=105627547 {ECO:0000313|EnsemblMetazoa:XP_012064219.1};
OS Atta cephalotes (Leafcutter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012064219.1, ECO:0000313|Proteomes:UP000005205};
RN [1] {ECO:0000313|Proteomes:UP000005205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA Weinstock G.M., Gerardo N.M., Currie C.R.;
RT "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT insights into its obligate symbiotic lifestyle.";
RL PLoS Genet. 7:e1002007-e1002007(2011).
RN [2] {ECO:0000313|EnsemblMetazoa:XP_012064219.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (APR-2016) to UniProtKB.
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DR EMBL; ADTU01007760; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012064219.1; XM_012208829.1.
DR AlphaFoldDB; A0A158P361; -.
DR STRING; 12957.A0A158P361; -.
DR EnsemblMetazoa; XM_012208829.1; XP_012064219.1; LOC105627547.
DR GeneID; 105627547; -.
DR KEGG; acep:105627547; -.
DR eggNOG; KOG0817; Eukaryota.
DR InParanoid; A0A158P361; -.
DR OrthoDB; 5402066at2759; -.
DR Proteomes; UP000005205; 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 InterPro; IPR022408; Acyl-CoA-binding_prot_CS.
DR InterPro; IPR000582; Acyl-CoA-binding_protein.
DR InterPro; IPR035984; Acyl-CoA-binding_sf.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR PANTHER; PTHR23310; ACYL-COA-BINDING PROTEIN, ACBP; 1.
DR PANTHER; PTHR23310:SF77; LD25952P; 1.
DR Pfam; PF00887; ACBP; 1.
DR PRINTS; PR00689; ACOABINDINGP.
DR SUPFAM; SSF47027; Acyl-CoA binding protein; 1.
DR PROSITE; PS00880; ACB_1; 1.
DR PROSITE; PS51228; ACB_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005205};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 327..345
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 3..92
FT /note="ACB"
FT /evidence="ECO:0000259|PROSITE:PS51228"
FT REGION 154..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 270..297
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 154..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 353 AA; 40300 MW; 6FADF1D7145FEE7B CRC64;
MTTEEKFNAA VNVIRSLPKN GAYQPSHEIM LRFYSYYKQA TEGPCQQSKP AFWEVVKKAK
WDAWTRLGNM SRTEAMNNYV EELKKIVETM SYTDNVATFL GSLDSFYESV PAEDLELLVG
PVLERIRSQP GSPLSGSPLV SRETSPHRVI NASRHITSSL ETSPTSSRTA SPLPQDTDGE
EEEFIDTVES APERAQKDAL KSTIASQKVQ TMAKNGIDHS STENIIKENI ELTNGYSNTN
GYAETISENH RERSRQRTKK DDNKANAEFL NQIATTMQHL QRDLDRITAR VRGLEGQALQ
ALAPSPEHTV RRKYLKWWPL QECPPRLFVL LILWPFVAHL LINFMQRYRQ RRL
//
