ID A0A0R3SWS8_HYMDI Unreviewed; 688 AA.
AC A0A0R3SWS8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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|RuleBase:RU368023};
GN ORFNames=HDID_LOCUS10153 {ECO:0000313|EMBL:VDL62790.1};
OS Hymenolepis diminuta (Rat tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Hymenolepididae; Hymenolepis.
OX NCBI_TaxID=6216 {ECO:0000313|Proteomes:UP000046397, ECO:0000313|WBParaSite:HDID_0001015501-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HDID_0001015501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDL62790.1, ECO:0000313|Proteomes:UP000274504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of complexes involved in DNA repair and protein
CC ubiquitination. May play a role in the regulation of the circadian
CC clock. {ECO:0000256|RuleBase:RU368023}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|RuleBase:RU368023}.
CC -!- SUBUNIT: Component of the UV-DDB complex.
CC {ECO:0000256|RuleBase:RU368023}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU368023}.
CC -!- DOMAIN: The core of the protein consists of three WD40 beta-propeller
CC domains. {ECO:0000256|RuleBase:RU368023}.
CC -!- SIMILARITY: Belongs to the DDB1 family.
CC {ECO:0000256|RuleBase:RU368023}.
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DR EMBL; UYSG01011547; VDL62790.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R3SWS8; -.
DR STRING; 6216.A0A0R3SWS8; -.
DR WBParaSite; HDID_0001015501-mRNA-1; HDID_0001015501-mRNA-1; HDID_0001015501.
DR Proteomes; UP000046397; Unplaced.
DR Proteomes; UP000274504; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR018846; Cleavage/polyA-sp_fac_asu_N.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR10644:SF3; DNA DAMAGE-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR10644; DNA REPAIR/RNA PROCESSING CPSF FAMILY; 1.
DR Pfam; PF10433; MMS1_N; 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|RuleBase:RU368023};
KW DNA repair {ECO:0000256|RuleBase:RU368023};
KW Nucleus {ECO:0000256|RuleBase:RU368023};
KW Reference proteome {ECO:0000313|Proteomes:UP000274504}.
FT DOMAIN 78..588
FT /note="Cleavage/polyadenylation specificity factor A
FT subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10433"
SQ SEQUENCE 688 AA; 76150 MW; 92E089FED6941498 CRC64;
MFVYTVALFN GISKIVYING CGNGNFTGPN DLNLVFIKNS YIEIYDITSE GLRVVRDIPL
NGTILTALLF RRRNRKQDSL CIVTLRADLI VLECVRTKDS IDFVTVFRKN IDSRGHHLLH
HGVTAMVDPT STYIAIRLFH NLMKLVEINH LPERPGVKVE ESKIHAVKLD EGNVIDLTFI
NGYGYPTFAM ICEDQGAAHL RMYELNTKDH ILVPLPANFS AIETTSRMLV PVAAPYYGFL
VVGDEMISYH SPNKPHITTC IPQKTVSVIC SCKVALVSSS AHLYLLSKVV AYAQVDNKRY
LMGNLCGELF MVHLVGPEVD ALAPLSAVLE RLRIERLGIT SVPESIVYLD KGVVFIGSYF
GDSQLIHLRS DIDPDTKCYF DVYEEYPNLG PIADMIFVEN EGQNQLITCS GYSRDGSLRI
IRNGIGIQEI ATIGQEHMNG VWCIPCNSEV YDDAMICSMK RRSRIVRVIG DDLAGLKLEG
FVRDDRTLYC NTVHPQGYKK SPRPLLLQAT NDTLWLIGIQ DLYGKGCLAT WKPPTGMSLS
SLTARGDLVI VASGNCIFAL RITGTPEKPV FTQVGQNELA CEIACIDITP FNKSKSADSS
TAAAGDILGD MEPEYAAVGL WLGHGICLLK LPSLEQVFND PLPKEIRSTG AVILPRSIAI
AQFDELLYVF CVSGDGTLFY YNVDYSNG
//