ID   A0A3P6T5I9_LITSI        Unreviewed;      1181 AA.
AC   A0A3P6T5I9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=DNA damage-binding protein 1 {ECO:0000256|ARBA:ARBA00014577, ECO:0000256|RuleBase:RU368023};
DE   AltName: Full=Damage-specific DNA-binding protein 1 {ECO:0000256|ARBA:ARBA00031668, ECO:0000256|RuleBase:RU368023};
GN   ORFNames=NLS_LOCUS6113 {ECO:0000313|EMBL:VDK83236.1};
OS   Litomosoides sigmodontis (Filarial nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Litomosoides.
OX   NCBI_TaxID=42156 {ECO:0000313|EMBL:VDK83236.1, ECO:0000313|Proteomes:UP000277928};
RN   [1] {ECO:0000313|EMBL:VDK83236.1, ECO:0000313|Proteomes:UP000277928}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a role in DNA repair. May be a component of an E3
CC       ubiquitin-protein ligase which promotes histone ubiquitination in
CC       response to UV irradiation. Histone ubiquitination may be important for
CC       subsequent DNA repair. {ECO:0000256|RuleBase:RU368023}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|RuleBase:RU368023}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU368023}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU368023}.
CC   -!- SIMILARITY: Belongs to the DDB1 family. {ECO:0000256|ARBA:ARBA00007453,
CC       ECO:0000256|RuleBase:RU368023}.
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DR   EMBL; UYRX01000513; VDK83236.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3P6T5I9; -.
DR   STRING; 42156.A0A3P6T5I9; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000277928; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.150.910; -; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
DR   InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C.
DR   InterPro; IPR018846; Cleavage/polyA-sp_fac_asu_N.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR10644:SF3; DNA DAMAGE-BINDING PROTEIN 1; 1.
DR   PANTHER; PTHR10644; DNA REPAIR/RNA PROCESSING CPSF FAMILY; 1.
DR   Pfam; PF03178; CPSF_A; 1.
DR   Pfam; PF10433; MMS1_N; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|RuleBase:RU368023};
KW   Nucleus {ECO:0000256|RuleBase:RU368023};
KW   Reference proteome {ECO:0000313|Proteomes:UP000277928}.
FT   DOMAIN          75..564
FT                   /note="Cleavage/polyadenylation specificity factor A
FT                   subunit N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10433"
FT   DOMAIN          822..1132
FT                   /note="Cleavage/polyadenylation specificity factor A
FT                   subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03178"
SQ   SEQUENCE   1181 AA;  131268 MW;  E9A9F17E95AE0894 CRC64;
     MALNYIVTAY KPTVVTHAVV GSFIIPTELN LVLAKTNRVE LFLVKPEGLK PHRECPVFGR
     IATMKLFRVP GENVDSLLIL TAKYHLAIIR WTSTSELRTR ASGHIVDRVG RPSETGMIAT
     VHPSGLMVFR LYDGLLKVVQ WNEGKDLRGF NVRCDDLYII DVAFLADPDR PTLAYIYQDD
     NGRHVKVVTV NVGDKELSSP LWRHDNLEGE ANMVISVPEP VGGCLIASPD AISYHKGGED
     AMRYVGMPGS KLHNTHPNCF APVDRDGQRY LLADLAGNLY MLLLELGKDE EQDESSAITV
     RDMKVESLGE TCIAECMCYL DNGVCFIGSR FGDSQLIRLN TEPRADGTGY VSLLDSYTNL
     APIRDMTVMR CNGQQQILTC SGAYKDGTIR IIRNGIGIEE LASVELKGIK NMFTLRTQNQ
     EFDDYLILSF DSETHILFIN GEELVDTQIT GGEFCTGYVS FINVVLASPF QRSFTTNGAT
     LWAGCLFCTK TILQVTHGEA ILINDGNIQV WKAPKWITLL AVNEITGQLV IVCGALLIYL
     EADAAGFKVI NELECEFEVS CIDITPVGNN SERSEICAVG YWTDLSVALR TLPQLEEVVR
     EKIVGDMLSR SIMLSSMEGH VYLLVALGDG TVHYFQIDMK TGALFDPKKA TLGTQPIHLR
     KFRSRCSPIQ NIFVCSDRPA VIYSSNQKLL FSNVNLRMVS TMTPLCSGAY SDALVLTDGY
     SLVIVKQTLP KKPVVFPGRI DDIQKLHIRT VPLGESPSRI AYQSETNTIA VIVERLEFVD
     SMGKHHSGQC ASKSAMETSS SRLSSMRREP TQECLAEEME VSSILLMDSN TFEVLHSHEL
     EGNEMAMSLT SCKLGNDIQP YFVVGTAVIM SDETESKMGR IMMFQASEGP ERMRLVYEKE
     IKGAAYSIQP MDGKLVVAVN SCVRLFEWTA DKELRLECSD FDNVTALYLK TKNDLILVGD
     LMRSLSLLSY KSMESTFEKV ARDFMTNWMS ACEIIDSDNF LGAENSYNLF TVIKDSFTIF
     KEEGTRLQEL GLFYLGEMVN VFCHGSLTAT QVDVAPLYHS SILYGTSDGG IGAVVQMPPA
     VFAFLQDVQK RLAEQTENCM RISHTQYRTF ETEKRSEAPN GFIDGDLIES LLDMGKDLVE
     QIVKGLKMPL LISMPASEST ELVDVTAEDV LKLVEDLSRI H
//