ID W5NGF7_LEPOC Unreviewed; 504 AA.
AC W5NGF7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Aprataxin and PNKP like factor {ECO:0000313|Ensembl:ENSLOCP00000019716.1};
GN Name=APLF {ECO:0000313|Ensembl:ENSLOCP00000019716.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000019716.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000019716.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AHAT01001627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5NGF7; -.
DR Ensembl; ENSLOCT00000019748.1; ENSLOCP00000019716.1; ENSLOCG00000016006.1.
DR GeneTree; ENSGT00390000010591; -.
DR Proteomes; UP000018468; Linkage group LG16.
DR Bgee; ENSLOCG00000016006; Expressed in ovary and 13 other cell types or tissues.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:InterPro.
DR GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR CDD; cd22717; FHA_APLF; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR InterPro; IPR039253; APLF.
DR InterPro; IPR019406; APLF_PBZ.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR21315:SF2; APRATAXIN AND PNK-LIKE FACTOR; 1.
DR PANTHER; PTHR21315; UNCHARACTERIZED; 1.
DR Pfam; PF10283; zf-CCHH; 2.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT DOMAIN 367..392
FT /note="Aprataxin and PNK-like factor PBZ"
FT /evidence="ECO:0000259|Pfam:PF10283"
FT DOMAIN 409..433
FT /note="Aprataxin and PNK-like factor PBZ"
FT /evidence="ECO:0000259|Pfam:PF10283"
FT REGION 131..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..483
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 504 AA; 55629 MW; 5B2F0BACB45C1865 CRC64;
MSGFELEPLD GNCSIPLPVG ETLIGRGPLL RVSDKRVSRN HGLLEVVDGQ LRIKPTHLNP
CFYQSSLDDL PHPLEKDKWH PLFPGDLFSL LPGKYIYRVV STNCDSTQSF SPRNSQALAR
NDLRDKTLGL TQEYPETSGS SIEKECKAKT DVPPSKNIGG SAEGGRTEEG KSMQRKRVLP
AWMLQGAAGA QRTLKSTGDA ACFNVEMENG EKQGRSKLSP EQSKGTGSRS QLTSSKGIEE
TDTRPASPGR KPKRKKCEES TVEAHLYPQA TSSAADNGRI RREDEHIEES DKVSGRLSDD
EELRHVPAGK SDPHSKSREV DLSDSEEKEG PSQRPLQRKG QGTLPKATGS SGSASPMMAG
TSRKQPRNPC MYGTNCYRKN PVHFQEFSHP GDSDYEEKSA VSDDASDCRP ECPYGTDCYR
KNPQHRKEYR HTKASGKKSA LAGDDDDGEP NDYDLNDSFI DDEELEDSDH SDEDSDYVPD
SDDSVAEDLN TLSKEAKEFM GRKK
//
