GenomeNet

Database: UniProt
Entry: F4WMP3_ACREC
LinkDB: F4WMP3_ACREC
Original site: F4WMP3_ACREC 
ID   F4WMP3_ACREC            Unreviewed;       643 AA.
AC   F4WMP3;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Homeobox protein araucan {ECO:0000313|EMBL:EGI64520.1};
DE   Flags: Fragment;
GN   ORFNames=G5I_07027 {ECO:0000313|EMBL:EGI64520.1};
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:EGI64520.1}
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PROSITE-ProRule:PRU00108}.
CC   -!- SIMILARITY: Belongs to the TALE/IRO homeobox family.
CC       {ECO:0000256|ARBA:ARBA00008446}.
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DR   EMBL; GL888218; EGI64520.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4WMP3; -.
DR   STRING; 103372.F4WMP3; -.
DR   EnsemblMetazoa; XM_011057717.1; XP_011056019.1; LOC105147013.
DR   eggNOG; KOG0773; Eukaryota.
DR   InParanoid; F4WMP3; -.
DR   Proteomes; UP000007755; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0048646; P:anatomical structure formation involved in morphogenesis; IEA:UniProt.
DR   GO; GO:0001654; P:eye development; IEA:UniProt.
DR   CDD; cd00086; homeodomain; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR008422; Homeobox_KN_domain.
DR   InterPro; IPR003893; Iroquois_homeo.
DR   PANTHER; PTHR11211:SF40; HOMEOBOX PROTEIN ARAUCAN-RELATED; 1.
DR   PANTHER; PTHR11211; IROQUOIS-CLASS HOMEODOMAIN PROTEIN IRX; 1.
DR   Pfam; PF05920; Homeobox_KN; 1.
DR   SMART; SM00389; HOX; 1.
DR   SMART; SM00548; IRO; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU00108};
KW   Homeobox {ECO:0000256|ARBA:ARBA00023155, ECO:0000256|PROSITE-
KW   ProRule:PRU00108};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00108}; Reference proteome {ECO:0000313|Proteomes:UP000007755}.
FT   DOMAIN          182..245
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000259|PROSITE:PS50071"
FT   DNA_BIND        184..246
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          99..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          246..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          333..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          381..448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          491..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..358
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        491..508
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        549..618
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EGI64520.1"
SQ   SEQUENCE   643 AA;  67067 MW;  F91090D4F84F2435 CRC64;
     QLLVSGGQPT TATSPAMSGG ALSPGALSPS STATTTTGVG PAGTGGATTP VGGAATGPGC
     CENGRPMMTD PVTGQTVCSC QYDNAARFAL STYPRLPTAT SYSSYPTPTP STTDQGPYPS
     IGMDSSAFYS PLGNPYGLKD ATGMGMTADM GAAWGTAALQ PAATGYYPYD PTLAAYGYGA
     GYDLAARRKN ATRESTATLK AWLNEHKKNP YPTKGEKIML AIITKMTLTQ VSTWFANARR
     RLKKENKMTW EPKNKTDDDD DAVLTDSEDN KEKDDLASDN RGDRVSEDAR RGLDDTEPMR
     HVKAELLQHE KDLDDEDELD LEDDRRRSEH PFHHTMQHHH HHHQGYGGED HLKEEGIKSD
     CSGGGVPIPA TKPKIWSLAD TAACKTPPPP SHPHHQQYHH LHHQQHYPQQ QQQHHVPNQG
     HHHHSQQPWL GPGGAGGGAG SGGGGGNLGS SFALPSSAGM SPSAAATAPY SGAAARYGGF
     LSSSSGGQLH YNPNSSSGSS SSASSSAAAA AGFPEVGTDT PPQTPPNMKV ATPNGVIQAP
     PGGYCPGGNT ASAATNGNPN IPYGANHPGS GYLSSSSGST SSASSFNSRL QSSPHKDFSS
     VGQNSILHQH QTTASLPPTE ATTAFKPFYK GSQSMGSGFV SPV
//
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