ID   A0A2A3EQ74_APICC        Unreviewed;      1138 AA.
AC   A0A2A3EQ74;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=APICC_03883 {ECO:0000313|EMBL:PBC33915.1};
OS   Apis cerana cerana (Oriental honeybee).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Apis.
OX   NCBI_TaxID=94128 {ECO:0000313|EMBL:PBC33915.1, ECO:0000313|Proteomes:UP000242457};
RN   [1] {ECO:0000313|EMBL:PBC33915.1, ECO:0000313|Proteomes:UP000242457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Pupae without intestine {ECO:0000313|EMBL:PBC33915.1};
RA   Diao Q., Sun L., Zheng H., Zheng H., Xu S., Wang S., Zeng Z., Hu F., Su S.,
RA   Wu J.;
RT   "Genomic and transcriptomic analysis on Apis cerana provide comprehensive
RT   insights into honey bee biology.";
RL   Submitted (JUL-2014) 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; KZ288194; PBC33915.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A3EQ74; -.
DR   STRING; 94128.A0A2A3EQ74; -.
DR   Proteomes; UP000242457; 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   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:UP000242457}.
FT   DOMAIN          75..542
FT                   /note="Cleavage/polyadenylation specificity factor A
FT                   subunit N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10433"
FT   DOMAIN          788..1097
FT                   /note="Cleavage/polyadenylation specificity factor A
FT                   subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03178"
SQ   SEQUENCE   1138 AA;  126217 MW;  EF6E4C4AC0193C3F CRC64;
     MSHHYVVTAH KPTAVTACVT GNFTSPTDLN LILAKNVRLE IYLVTPEGLR PLKEVGIYGK
     IAVVKFFRPP HEKKDLLFLL TTRYNAMILE CIGEGENIEI ITKAHGNVAD RIGKASETGI
     KAVIDPKARV IGLRLYDGLF KIIPLDKDNP ELKASSIRME EHQVQDVNFL HGCANPTLIL
     IHQDINGRHV KTHEISLRDK EFVKIPWRQD NVEREAMIVI PVPSPICGAI IIGQESILYH
     DGNTYVAVVP PIIKQSTITC YAKVDNQGLR YLLGDMAGHL FMLFVEQEKK ADGTQVVKDL
     KVELLGEISI PECITYLDNG VIFVGSRLGD SQLVKLITKA DENGSYCVPM ETFTNLAPIV
     DMAVVDLERQ GQGQMVTCSG AFKEGSLRII RNGIGIEEHA SIDLPGIKGM WALKIGGGNF
     DNTLVLSFVG QTRILTLNGE EVEETDIPGF VADEQTFHTG NVTNDLFIQI TPTSARLISY
     ETKTVVSEWE PENKRTISVV ACNGTQVLCA TGNDLFYLEI SCGQILPKGF TTLQYEVACL
     DISPLDGNTE AKIAAVGLWT HISVHILTLP ALEEINKELL GGEIIPRSIL MTCFEGNTYL
     LCALGDGSMY YFTLHKQNGI LSDKKKVTLG TQPTVLRTFR SLFTTNVFAC SDRPTVIYSS
     NHKLVFSNVN LKEVNHMCSL NAESYPDSLA LATDSTVTIG TIDEIQKLHI RTVPLGESPR
     RIAYQESSQT FGVITMRVDI QDSSGVSIVR HSASTQAAST SSSSHIASYN KPTGHTASDI
     CQEIEVHNLL IIDQHTFEVL HAHMLMPTEY ALSLISTKLG EDPTSYYIVG TALVHPDETE
     PKMGRILLYH WSDGKLTQVA EKEIKGSCYS LTEFNGKLLA SINSTVRLFE WTAEKELRLE
     CSHFNNIIAL YLKSKGDFIL VGDLMRSLTL LQYKTMEGCF EEIARDYNPN WMTAIEILDD
     DTFLGAENCF NLFVCQKDSA ATSEDERQQM QEVGQFHLGD MVNVFRHGSL VMQNLGESST
     PTQGCVLFGT VSGAIGLVTQ IPFIFYEFLR NLEDRLTSVI KSVGKIEHNF WRSFNTELKI
     EQCEGFIDGD LIESFLDLSP DKMAEVASGL MIDDPSGMKK EATVDDLVKI VEDLTRIH
//