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Database: UniProt
Entry: A0A0V0S3B0_9BILA
LinkDB: A0A0V0S3B0_9BILA
Original site: A0A0V0S3B0_9BILA 
ID   A0A0V0S3B0_9BILA        Unreviewed;       622 AA.
AC   A0A0V0S3B0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Dystrobrevin {ECO:0000256|PIRNR:PIRNR038204};
GN   Name=dyb-1 {ECO:0000313|EMBL:KRX21270.1};
GN   ORFNames=T07_14834 {ECO:0000313|EMBL:KRX21270.1};
OS   Trichinella nelsoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX21270.1, ECO:0000313|Proteomes:UP000054630};
RN   [1] {ECO:0000313|EMBL:KRX21270.1, ECO:0000313|Proteomes:UP000054630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS37 {ECO:0000313|EMBL:KRX21270.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|PIRNR:PIRNR038204}.
CC   -!- SIMILARITY: Belongs to the dystrophin family. Dystrobrevin subfamily.
CC       {ECO:0000256|ARBA:ARBA00009563, ECO:0000256|PIRNR:PIRNR038204}.
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:KRX21270.1}.
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DR   EMBL; JYDL01000040; KRX21270.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0S3B0; -.
DR   STRING; 6336.A0A0V0S3B0; -.
DR   Proteomes; UP000054630; 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; 1.
DR   SMART; SM00291; ZnF_ZZ; 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   Cytoplasm {ECO:0000256|PIRNR:PIRNR038204};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054630};
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          496..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          581..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          416..493
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        499..519
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   622 AA;  69899 MW;  C9A487FECE1FEA90 CRC64;
     MDTVDQNSTL SNSLAKNDFR MLVSDLREQN FDTIRFATYR AACKLRFIQQ KVNLHLVDIW
     NVIESFRENG LNAVEYKSEV KISRVELLLS TVYHNLNKRL PVVQQIDSDL TIRLLISFLV
     AAFDRDDNGK LQVFSVKVAL ATLCAGKLLD KLRYIFSLIS DTSGVMDFNR FCDYLKEVLC
     LPCAVFEGPT FSYSESLPKQ IFDPSAKVTI NTFLDALMAD PCPPCLMWLP LLHRMASVEH
     VFHPVVCDAC NRDSFTGFRY KCQRCHNYQL CQDCFWRGRI SDSHTNQHEM KEYSSYKSPT
     KQLGHSISKS LQCVPGHTNK KPYVPEVSER PLDLSNAVPS SPSLVRCLLK KNSEINPTDN
     SIDGSRPCLV STCWYDNLDD EHKLIARYTA KLSGRSTYRP AATNAAEENL AQRATIAHLE
     KKNREILREI HRLQAMQSAT NLSMMSTSAV GENGATVELD NLRLRKTELE IRMQQLQDTR
     KDLLMQLEGL MKVLKTQLPR DNSPRSLLQA SNNDADSKAK DVGNVNDADS SLYGGTCGRL
     AQQFLPSSPY SSFGPRKSSL QSDLLSAADS ITNTMTSLVQ ELNTAETEAE EQNGTPTTAT
     TTTACNEQQQ QDEGNERSTT TT
//
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