ID   A0A836JWA0_9HYME        Unreviewed;      1300 AA.
AC   A0A836JWA0;
DT   29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 1.
DT   02-APR-2025, entry version 13.
DE   SubName: Full=HTS protein {ECO:0000313|EMBL:KAG5328131.1};
DE   Flags: Fragment;
GN   Name=Hts {ECO:0000313|EMBL:KAG5328131.1};
GN   ORFNames=G6Z76_0014152 {ECO:0000313|EMBL:KAG5328131.1};
OS   Acromyrmex charruanus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Acromyrmex.
OX   NCBI_TaxID=2715315 {ECO:0000313|EMBL:KAG5328131.1, ECO:0000313|Proteomes:UP000669903};
RN   [1] {ECO:0000313|EMBL:KAG5328131.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BGI-DK2014a {ECO:0000313|EMBL:KAG5328131.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KAG5328131.1};
RA   Bi X.;
RT   "Relaxed selection underlies rapid genomic changes in the transitions from
RT   sociality to social parasitism in ants.";
RL   Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004413};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413};
CC       Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}.
CC   -!- SIMILARITY: Belongs to the aldolase class II family. Adducin subfamily.
CC       {ECO:0000256|ARBA:ARBA00006274}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAG5328131.1}.
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DR   EMBL; JAANIC010006835; KAG5328131.1; -; Genomic_DNA.
DR   Proteomes; UP000669903; Unassembled WGS sequence.
DR   GO; GO:0005856; C:cytoskeleton; IEA:TreeGrafter.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0014069; C:postsynaptic density; IEA:TreeGrafter.
DR   GO; GO:0051015; F:actin filament binding; IEA:TreeGrafter.
DR   FunFam; 3.40.225.10:FF:000011; Uncharacterized protein, isoform B; 1.
DR   Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 1.
DR   InterPro; IPR051017; Aldolase-II_Adducin_sf.
DR   InterPro; IPR001303; Aldolase_II/adducin_N.
DR   InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR   PANTHER; PTHR10672; ADDUCIN; 1.
DR   PANTHER; PTHR10672:SF3; PROTEIN HU-LI TAI SHAO; 1.
DR   Pfam; PF00596; Aldolase_II; 1.
DR   SMART; SM01007; Aldolase_II; 1.
DR   SUPFAM; SSF53639; AraD/HMP-PK domain-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000669903}.
FT   DOMAIN          126..308
FT                   /note="Class II aldolase/adducin N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01007"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          588..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          957..994
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..13
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        602..626
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        969..979
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KAG5328131.1"
FT   NON_TER         1300
FT                   /evidence="ECO:0000313|EMBL:KAG5328131.1"
SQ   SEQUENCE   1300 AA;  146165 MW;  AACB2C9D048F8CA6 CRC64;
     MADTSQQALS EPHTNGVVDG LTEDEKSKMR PADIDADMRE MERRKRVEMM MNSRIFREEL
     ERIIETQMRD GAGPSGLLQQ ISDMMGAQGA RFNGNVFKNS NCVLPINDIR GVESMGYAKG
     EKLLRCKMAA VFRLLDLYGW TQGVGGQITA RLNQDEEHFL VNPYGLLYHE VTASSLIKVD
     MQGTIVEQGT TNFGVHITGF QLHSTIHAAR PDIKCIIHIT TPSVTAVSSL KCGLLPIGQE
     SIVIGEVSTH QYIGGSVEPE EREKIARNLG PINKVMLLTN RGALCCGETV EEAFFNVYNT
     VVACETQLKL MPAGVDNLSL ISEESKKAIF EASRKPPIPQ QQSSVVESSA LAEKLEKRWR
     IGGAEFEALM RMLDNAGFRT GYIYRNPLVK GEPPKPRNDV EVPPAVSSLG YLLEEEELYK
     QGLWKGGRKG TDRSRWLNSP NVYQKVEILE TGTPDPKKIT KWVSDGSPTH SSTPVKIDSA
     LQFVPKNTNP KEFKQLQQQI KDYRRAEKIS AGPQSHILEG VSWEEAKKMQ DATISGTGEQ
     VVLVGAASKG IIQRGFQHNA MVYKTPYAKN PFDAVTDQEL DQYKREVERK QKGDPYDESQ
     SESEALSSFN ISRATHESST AKSPIQSPVS VTSETEEESR DEPRVLRIET KQVPVPSQPE
     VVLSDVNDAT TEYLNEMRYR MTERQSGYKG DCELASNYSS VSSECARKYY GRRFSEHPYD
     NPRLENVRAS TTAERKKPLL ITRTKTLVNG QNEPNAISRD EVFVKSRYEV RRKFFEDLER
     QKNLETDLTT AKITSINSKE NELILERNSM MNPSENAHLV KFCAETFQHD NGDNKEDTRL
     LSNLSFNICD GHSIDRYECD DNETLDKEIN DELKPTELKK QSVRSWIESS MYEDNWPNDV
     KTDLYESYND IAKIVESIDV NITSSRTELD ALPDTDTCVK YNLDSTNMSL IYSLTPPAAV
     DQDESGNDDT SRDLADRSSE WQSDSTRSDN DEPLSDYIWI EPDTFTTKAE CVKFTRDHRL
     SSDSSCAELE LLESERHSAS GSDILELPSC TIRELNDIDG EVFLNGINES ANEIIADLNA
     SNEVLPSSDA IEVVQQIIAE IIESIYILLQ LDSSIHDLSI VREIVRNLIN NYHRECSLPK
     DDESPAVIEF CTVAKKLPIV TIDNSALELN FRVIKVSTDE YANMDKTSCL TPISEEPDDT
     LHEVVDSVTP TLKIHDESLE GRDIIEENTT ANPARKHISL DDTYTISEVS SVVISDNEMN
     DLEEQCNVWD TSIDCMSYSY ETKEFMRLEK ALADKSQLSA
//