ID F4WDF7_ACREC Unreviewed; 343 AA.
AC F4WDF7;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Regulatory protein zeste {ECO:0000256|ARBA:ARBA00016807};
GN ORFNames=G5I_03610 {ECO:0000313|EMBL:EGI67737.1};
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:EGI67737.1}
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.
CC -!- FUNCTION: Involved in transvection phenomena (= synapsis-dependent gene
CC expression), where the synaptic pairing of chromosomes carrying genes
CC with which zeste interacts influences the expression of these genes.
CC Zeste binds to DNA and stimulates transcription from a nearby promoter.
CC {ECO:0000256|ARBA:ARBA00025466}.
CC -!- SUBUNIT: Self-associates forming complexes of several hundred monomers.
CC {ECO:0000256|ARBA:ARBA00011764}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the ATPase inhibitor family.
CC {ECO:0000256|ARBA:ARBA00010901}.
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DR EMBL; GL888087; EGI67737.1; -; Genomic_DNA.
DR AlphaFoldDB; F4WDF7; -.
DR STRING; 103372.F4WDF7; -.
DR EnsemblMetazoa; XM_011052478.1; XP_011050780.1; LOC105143909.
DR EnsemblMetazoa; XM_011052585.1; XP_011050887.1; LOC105143968.
DR eggNOG; ENOG502S8MH; Eukaryota.
DR InParanoid; F4WDF7; -.
DR Proteomes; UP000007755; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0042030; F:ATPase inhibitor activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR Gene3D; 1.20.5.500; Single helix bin; 1.
DR InterPro; IPR007648; ATPase_inhibitor_mt.
DR InterPro; IPR028002; Myb_DNA-bind_5.
DR PANTHER; PTHR21411; APONTIC; 1.
DR PANTHER; PTHR21411:SF0; REGULATORY PROTEIN ZESTE; 1.
DR Pfam; PF04568; IATP; 1.
DR Pfam; PF13873; Myb_DNA-bind_5; 1.
DR SUPFAM; SSF64602; F1 ATPase inhibitor, IF1, C-terminal domain; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000007755}.
FT DOMAIN 17..92
FT /note="Myb/SANT-like DNA-binding"
FT /evidence="ECO:0000259|Pfam:PF13873"
FT REGION 128..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 301..342
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 128..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 343 AA; 39316 MW; C409A081F37006A7 CRC64;
MSTTSETTTV LLKKRERTQN WIPEEKSALF SLIKHHVSAI ENKKIDAAAS AKKSVAWQKI
YCAFRGQFSA DRDITRIKEQ WRRMKAQARM EMFSYAEKVR TLGPDVAAKS RPPNLSIEVW
RLMESVRKND SENTDRSDDS QDNENPLNRM AIQAILDKLT LPTETPEPEQ EIKIEVNSDT
EDESNHGELS RQVSEDYFLQ QKRPRIKIQG EPVDLEHRIT CPDSLSTSRV ENEYFVIGKM
QRTITTFSRS ISALSQVRMV GERGSGAGKG GGGGGAVRDA GGSFGKMEAA HEDQYFYNLQ
KEQLQKMRES LHDEISFHEE QIKRHQEAIN RHKKRITDMD QKE
//
