ID A0A368H9D5_ANCCA Unreviewed; 567 AA.
AC A0A368H9D5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Dystrobrevin {ECO:0000256|PIRNR:PIRNR038204};
GN ORFNames=ANCCAN_00749 {ECO:0000313|EMBL:RCN53194.1};
OS Ancylostoma caninum (Dog hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=29170 {ECO:0000313|EMBL:RCN53194.1, ECO:0000313|Proteomes:UP000252519};
RN [1] {ECO:0000313|EMBL:RCN53194.1, ECO:0000313|Proteomes:UP000252519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Baltimore {ECO:0000313|EMBL:RCN53194.1,
RC ECO:0000313|Proteomes:UP000252519};
RA Mitreva M.;
RT "Draft genome of the hookworm Ancylostoma caninum.";
RL Submitted (OCT-2014) 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:RCN53194.1}.
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DR EMBL; JOJR01000003; RCN53194.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368H9D5; -.
DR STRING; 29170.A0A368H9D5; -.
DR Proteomes; UP000252519; 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:UP000252519};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 246..302
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT COILED 418..466
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 567 AA; 63750 MW; AC9B73B11FB25562 CRC64;
MWSNGDVQPE ISGSTAPDCS GEMQALIDEM RVQDFDSIRF ATYRAACKLR FIQKKTNVHL
VDIWNMIESF RENGLNAMPI HTQIKTSRIE LLLTTIYHNL NKRLVSSQHI DTDKSISLLL
SFLLGTYDKQ QTGRLTVFSI KIALATICAG KLVDKLRYMF SQISDSSGFL EYDKFTDFLQ
QVLALTTAVF EAPTFGFSEA AVAQCFLKDQ RVTLNNFLDV FMSDPCPPCV MWLPLLHRMA
SVEHVYHPVV CDACQVRSFT GFRYKCQRCT NYQLCQNCFW RGRTSQNHSN EHEMKEYSSY
KSPTKQLAHS IHKSLQCIPT ANTKPPPLFA ERPQRPLELQ NIVPATPTTL RRAPPDPIPD
WPSSPVLLPG QVANGAALDD EHKLIARYSA KLSGRADYPL GNGRDRSINH PVDERSLIAR
LEEENSHMMR EISRLESQTL SDDGQLTGLR ERKSQLEEKM FVMQQKRRDL MMQLEQLMTQ
LNAPGAVSYP SASMSQIPES LAGVGSKVSS AFRAGSLPAS ATNLQGDLLH AADQITTNMG
EFLRELDQAQ DQDVPASVPN GHYQGPI
//
