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Database: UniProt
Entry: A0A484BPW1_DRONA
LinkDB: A0A484BPW1_DRONA
Original site: A0A484BPW1_DRONA 
ID   A0A484BPW1_DRONA        Unreviewed;      1738 AA.
AC   A0A484BPW1;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Endonuclease {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AWZ03_003701 {ECO:0000313|EMBL:TDG49925.1};
OS   Drosophila navojoa (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7232 {ECO:0000313|EMBL:TDG49925.1, ECO:0000313|Proteomes:UP000295192};
RN   [1] {ECO:0000313|EMBL:TDG49925.1, ECO:0000313|Proteomes:UP000295192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Navoj_Jal97 {ECO:0000313|EMBL:TDG49925.1};
RC   TISSUE=Whole organism {ECO:0000313|EMBL:TDG49925.1};
RX   PubMed=30423125; DOI=.1093/jhered/esy059;
RA   Vanderlinde T., Dupim E.G., Nazario-Yepiz N.O., Carvalho A.B.;
RT   "An Improved Genome Assembly for Drosophila navojoa, the Basal Species in
RT   the mojavensis Cluster.";
RL   J. Hered. 110:118-123(2019).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC       membrane {ECO:0000256|ARBA:ARBA00004299}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004299}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004299}. Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004397}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
CC   -!- SIMILARITY: Belongs to the DNA/RNA non-specific endonuclease family.
CC       {ECO:0000256|ARBA:ARBA00010052}.
CC   -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008334}.
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:TDG49925.1}.
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DR   EMBL; LSRL02000019; TDG49925.1; -; Genomic_DNA.
DR   STRING; 7232.A0A484BPW1; -.
DR   OMA; LMRSEHE; -.
DR   Proteomes; UP000295192; Unassembled WGS sequence.
DR   GO; GO:0030127; C:COPII vesicle coat; IEA:InterPro.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   CDD; cd00091; NUC; 1.
DR   CDD; cd01479; Sec24-like; 1.
DR   Gene3D; 2.60.40.1670; beta-sandwich domain of Sec23/24; 1.
DR   Gene3D; 3.40.570.10; Extracellular Endonuclease, subunit A; 1.
DR   Gene3D; 1.20.120.730; Sec23/Sec24 helical domain; 1.
DR   Gene3D; 3.40.20.10; Severin; 1.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR   InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR   InterPro; IPR018524; DNA/RNA_endonuclease_AS.
DR   InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
DR   InterPro; IPR044929; DNA/RNA_non-sp_Endonuclease_sf.
DR   InterPro; IPR020821; Extracellular_endonuc_su_A.
DR   InterPro; IPR007123; Gelsolin-like_dom.
DR   InterPro; IPR036180; Gelsolin-like_dom_sf.
DR   InterPro; IPR044925; His-Me_finger_sf.
DR   InterPro; IPR006900; Sec23/24_helical_dom.
DR   InterPro; IPR036175; Sec23/24_helical_dom_sf.
DR   InterPro; IPR006896; Sec23/24_trunk_dom.
DR   InterPro; IPR012990; Sec23_24_beta_S.
DR   InterPro; IPR041742; Sec24-like_trunk_dom.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   InterPro; IPR006895; Znf_Sec23_Sec24.
DR   InterPro; IPR036174; Znf_Sec23_Sec24_sf.
DR   PANTHER; PTHR13803; SEC24-RELATED PROTEIN; 1.
DR   PANTHER; PTHR13803:SF4; SECRETORY 24CD, ISOFORM C; 1.
DR   Pfam; PF01223; Endonuclease_NS; 1.
DR   Pfam; PF00626; Gelsolin; 1.
DR   Pfam; PF08033; Sec23_BS; 1.
DR   Pfam; PF04815; Sec23_helical; 1.
DR   Pfam; PF04811; Sec23_trunk; 1.
DR   Pfam; PF04810; zf-Sec23_Sec24; 1.
DR   SMART; SM00892; Endonuclease_NS; 1.
DR   SMART; SM00477; NUC; 1.
DR   SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1.
DR   SUPFAM; SSF82754; C-terminal, gelsolin-like domain of Sec23/24; 1.
DR   SUPFAM; SSF81811; Helical domain of Sec23/24; 1.
DR   SUPFAM; SSF54060; His-Me finger endonucleases; 2.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   SUPFAM; SSF82919; Zn-finger domain of Sec23/24; 1.
DR   PROSITE; PS01070; NUCLEASE_NON_SPEC; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022759};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000295192};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          86..299
FT                   /note="DNA/RNA non-specific endonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00892"
FT   DOMAIN          87..299
FT                   /note="Extracellular Endonuclease subunit A"
FT                   /evidence="ECO:0000259|SMART:SM00477"
FT   REGION          516..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          608..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          679..973
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        539..558
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        569..588
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        683..707
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        708..743
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        784..801
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        825..841
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        858..872
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        884..949
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1738 AA;  191675 MW;  C8A2D11042B839D9 CRC64;
     MRRLWHLLGV AFGLASAVGC FLAGVYFQHT HATRQLQQLV QQDVYAYYIS PKIFAAFGFF
     NVPNGTPNHV QRIMKYGFPG LDDVRLYSDF VLSYDRRNRV AHWVCEHLQL ANLQGARGVG
     RASATYRADL SVPSNFRSTL ADYKHSGFDR GHLAAAGNHR GQQVHCNETF LLTNIAPQIG
     QGFNSGAWNK LEIYVRELAQ SFGSVYVCTG PLFKPRAQGN RKWTVEYQMI GENMVAVPTH
     FFKVIMVESR LPLGKPYMEA YVLPNAPIPN QSTLRDFLCD IREIEHFAGL HFFQGMRRSA
     IFGSNYPNPG AQSCAFYALA GLTGFVFGAY FQQESAIRQL FWMIKTDPYV FHHRRKLYPL
     VSTFRTDHED RLWNRSKCLT SKIRDRLIYA LFDMFNSIFF DKRPESLSPD LLDLIKYGLP
     STENLYVHKD YVVSQDLSTN APKWMCEHLK GNYRKLTTEA DGDALHLRYN DVYVLSCGAT
     RVCKAFKREI WRKLEEHVSQ MTEKYHSVPI YKEMNPNMYG PPSTQFQPQY PAGPPRGPTG
     WPSQQQQQQQ QQQPLQSQPP PQQQQPHQQP LQQPPTQQQQ QQYGAPVTSA QQPYVNGNYQ
     QQLTTSMSGL SVSGNPLKPS QPPVGMPTAA VSAPVAAPSG PFNQFNSNAP PTSQPMPPAS
     SGMNFNNNNN AYAAAYANGS TGPSPSPAPP VSAAAAGPSP SPAPSMYPPS SAASTMAQQT
     SAPGTMPQNV PGGVNQMTLN SASLAGLPHM PPKSSTQQLP PTSTAPGQPL PPVSQAGGYG
     RPGQPQMPPG PAAPAAFTQP GMPPQRPAAG VAPAAAFTQP GMVTQPPAAG GQNSNPYGVP
     PPGNFQGSYA GQPAPGPGPV QGAYPGAPPL PGQQAGPQQF GAAPPQPVGY PPQPGQQLQQ
     PSMPGYPPQP MPGYPPQAGQ QPQQPMPGYP PQPGSYPGQP GPGRPGYNQP PMPGAGSMYQ
     QAPPRRLDPD QMPNPIQVMI ENQQAAGGIF VTNQPGLLPP LVTTKFVVND QGNSSPRFIR
     SSLYCIPNTG DLLKTTALPL TLNISPLARI GKGEMEPPIV NFGDMGPIRC NRCKAYMSPN
     MQFVDAGRRF QCLMCKVTTE VHPDYYQHLD HTGQRVDKHE RPELLLGTYE FLATKDYCRN
     NTAPEVPAFI FIIDVSYNTI KSGLVHLLCS QIKNILKHLP VDQGQDKSKV RVGFITYNST
     VHFYNIKSSL AQPQMMVVGD VQEMFMPLLD GFLCHPEESA AVIDALMEEI PRMFVDTKET
     ETILYPAIQA GLEALKASNA SGKLLVFNST LPIAEAPGKL KNRDDRKLLG TDKEKTVLTP
     QTTVYNQLGQ ECVQQGCSVD LFVFNNAYID IATIGQVSRL TGGEVYKYTY FQAELDGKRL
     IEDIIKNVSR PIAFDAVMRV RTSAGIRPTE FFGHFYMSNT TDVELASIDA TKSVSIEIKH
     DDKLAPEENV YLQVALLYTS CSGQRRLRIL NLALRVTVTI ADVFKSCDLD AMMLFFAKQA
     CFKLMEHSPK QVKDNLIQRS AQILACYRKH CTSPTSAGQL ILPECLKLLP LYASCLLKND
     AVSGGSDMTL DDRSYVIQFV LAMDLNMSVN YLYPRFIPIH NVDVDESSLP TPVRCTHEKI
     TEDGAYILEN GVHLFVWLGQ SLSPTFVQSV FGVQCTQQVN AERFAIAADT PLARRITGII
     DQIMAERTRY MRVTCVRQND KLESVFRHFL IEDRGTDGSA SYVDFLCHMH KEIKDLLS
//
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