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Database: UniProt
Entry: A0A195ECJ2_9HYME
LinkDB: A0A195ECJ2_9HYME
Original site: A0A195ECJ2_9HYME 
ID   A0A195ECJ2_9HYME        Unreviewed;       786 AA.
AC   A0A195ECJ2;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Dystrobrevin beta {ECO:0000313|EMBL:KYN22933.1};
GN   ORFNames=ALC57_04716 {ECO:0000313|EMBL:KYN22933.1};
OS   Trachymyrmex cornetzi.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=471704 {ECO:0000313|EMBL:KYN22933.1, ECO:0000313|Proteomes:UP000078492};
RN   [1] {ECO:0000313|EMBL:KYN22933.1, ECO:0000313|Proteomes:UP000078492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tcor2-1 {ECO:0000313|EMBL:KYN22933.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN22933.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex cornetzi WGS genome.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the dystrophin family. Dystrobrevin subfamily.
CC       {ECO:0000256|ARBA:ARBA00009563}.
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DR   EMBL; KQ979074; KYN22933.1; -; Genomic_DNA.
DR   RefSeq; XP_018359372.1; XM_018503870.1.
DR   AlphaFoldDB; A0A195ECJ2; -.
DR   STRING; 471704.A0A195ECJ2; -.
DR   GeneID; 108758772; -.
DR   OrthoDB; 5405762at2759; -.
DR   Proteomes; UP000078492; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IEA:UniProt.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007154; P:cell communication; IEA:UniProt.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:UniProt.
DR   GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:UniProt.
DR   GO; GO:0023052; P:signaling; IEA:UniProt.
DR   CDD; cd16244; EFh_DTN; 1.
DR   CDD; cd02334; ZZ_dystrophin; 1.
DR   Gene3D; 3.30.60.90; -; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   InterPro; IPR017432; Distrobrevin.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR015153; EF-hand_dom_typ1.
DR   InterPro; IPR015154; EF-hand_dom_typ2.
DR   InterPro; IPR000433; Znf_ZZ.
DR   InterPro; IPR043145; Znf_ZZ_sf.
DR   PANTHER; PTHR12268:SF27; DYSTROBREVIN, ISOFORM F; 1.
DR   PANTHER; PTHR12268; E3 UBIQUITIN-PROTEIN LIGASE KCMF1; 1.
DR   Pfam; PF09068; EF-hand_2; 1.
DR   Pfam; PF09069; EF-hand_3; 1.
DR   Pfam; PF00569; ZZ; 1.
DR   PIRSF; PIRSF038204; Distrobrevin; 2.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1.
DR   SUPFAM; SSF47473; EF-hand; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078492};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00228}.
FT   DOMAIN          242..298
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50135"
FT   REGION          396..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          508..577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          701..724
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          738..786
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          427..498
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        400..414
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..548
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        549..577
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   786 AA;  87678 MW;  859C72FF578858EA CRC64;
     MAEEGAGGSG NGSSGETSRL QLLQEMRQQN FDTIRFASYR TACKLRFIQK KVHLHNVDIW
     NVIEAFRENG LNTLEPSSTL GVSRLETLLS SLFHALNKRV PVSQQSKVDA TTALLMNWLL
     AAYTSGENNK ISVFSVKVAL ATLCAGKLMD KFRYIYSQIS DSNGHMIHWR FADYLKEVLA
     LTAAVYESPS FGYSDGLANS IFPANSKVTV NDFLDTLMSD PGPHCLIWLP LYHRMATVET
     VAHPIMCDAC HKENFTGFRY RCQKCHSYQL CQDCFWRGKV SGTHNNDHET REYSSFKSPS
     KQIGHSLRKS FRCVPEKGKN SLPRFPEQPE KTLDLSHIVP PSPLPSHNGF PDPGFMAPFD
     SGSVDSRSTL RSMDSSRLDD EHKLIARYAQ RLAQEARTVP RTASRMSQAD QAGRAPSDVN
     LASLDASRAQ RELISQLEAK NKEIMREIAR LRRQQEIEAA GLENPALMSE LRALRQRKDE
     LETHLATLQD SRRQLMVQLE GLMKMLKNHQ ASPRSTPNSS PRSTKSPPLP PGAIPSSRSA
     PPTPGGPLST PQQQQQQQQQ HQQIQQQQMS QQMSQSYQNP IPTTVANVQG NAMLGTIQNP
     IPDSLSCVGG DVRSAFRTNS LPGSGSSSAN NSLGRSLRND LLVAADSVTN AMSTLVRELN
     SDVLWNVCDA PPVNVSWWLA DSDQEDHSHN SGLMNIRKPL DFEAGEDGDD SSGGGNSWRE
     ELQRRYQQEN DFLAELRSRN CIPQTPSATL SSEQEQERGE REEADGEKED EDEANWAEAV
     KRWVNR
//
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