ID B3RLC6_TRIAD Unreviewed; 1134 AA.
AC B3RLC6;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 71.
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=TRIADDRAFT_18324 {ECO:0000313|EMBL:EDV28743.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV28743.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV28743.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV28743.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
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. {ECO:0000256|ARBA:ARBA00007453,
CC ECO:0000256|RuleBase:RU368023}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS985241; EDV28743.1; -; Genomic_DNA.
DR RefSeq; XP_002107945.1; XM_002107909.1.
DR AlphaFoldDB; B3RLC6; -.
DR STRING; 10228.B3RLC6; -.
DR EnsemblMetazoa; TriadT18324; TriadP18324; TriadG18324.
DR GeneID; 6749937; -.
DR KEGG; tad:TRIADDRAFT_18324; -.
DR CTD; 6749937; -.
DR eggNOG; KOG1897; Eukaryota.
DR HOGENOM; CLU_002893_0_1_1; -.
DR InParanoid; B3RLC6; -.
DR OMA; HQDFLMR; -.
DR OrthoDB; 226997at2759; -.
DR PhylomeDB; B3RLC6; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0035861; C:site of double-strand break; IBA:GO_Central.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; 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; 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; PF03178; CPSF_A; 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:UP000009022}.
FT DOMAIN 75..544
FT /note="Cleavage/polyadenylation specificity factor A
FT subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10433"
FT DOMAIN 787..1094
FT /note="Cleavage/polyadenylation specificity factor A
FT subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03178"
SQ SEQUENCE 1134 AA; 125840 MW; F5615CE62B73DD4B CRC64;
MACNYVVTAH KPTAANASLF GNFTGPHDLN LIVAKNNRLD IQLVTAEGLV PLLDVGVYGR
IASMQLIRPE NENCDLLFIL TCRYRVCILQ YKPETKSIIT RAYGDMKNRV SRPSETGLIG
IVDPDCKVIC LKLYDGWLKL IPLELDTDKE MSAEDVRLEE LQVLDVKFLY GFTEPTIALI
YESGQNRYLK TYEISLQNAD IHRQPWNIGK VEEEAFMILP VPPPSCGMVV IGAGSISYYK
GQDSLHITPA SLKDRITCFG RVDSNGCRYL LGDYSGRLFM LILVQEHSQS GIKVKDLCLE
YLGETSIPSC ITYLDNAFAY IGSSCGDSQL IKVLNTSPDS ETDSYIDVID NFTNLGPIID
MVSVDLDKQG QSQLVTCSGF GKNASLRVLR NGIGIHELAN IDLDHICGIW RLRTVSRSIS
EYDDVLVLSF AGHSRFLKFD GREVEETDIS GFDDYKETDF AANVAFDQIV QISNESVRLA
GCDGRGLLQE WKPPNGKTIS KSTAGNTQIM VASGCELFYL EIGEGELKQV SNISLEHDIA
CIDISLKDDN ERAQICAVGL WVDMSARLLL LPNLQLMLTE SLGGDIIPRS IMLNRFDNEI
YLLVAMGDGT LAYYLVNTTT CSLTNRKSVN LGVVHSNLYT FKSGSISNVF ACSDRPTVIY
INNHKLVFSN VNLKKVNFMS PFHSESFPNS LALVNDSGFI IGTIDEIQKL HIRTKPLGET
TRQEESQSFG IITCRTEVPS EDDKNFVPTH QSASLLVSNR TMCPEQSDNS SSTFDSDTLS
EKNIDSVLII DQHSLDAQCA LQLQDCEWGM SLISCTFEND PEAYYCVGTA FVNLEDKEPT
KGNIRILKYF EGKIQQVHSK EVSGAVYCMV AFNGRLLASV NSTVSVYEWT SNKELVEETS
FHNNVLALYL KTKGDFILIG DLMRSISLCA YRPMNNEIEL ICKNNDPNWM TAVEIIDDDS
YLGGENSHNL FTCQKNSSSS EEEQKHLPTV GVYHVGEFVN VFRQGSLVMQ NTVDIPDSVQ
GSILFGTVSG AVGVVVTLAP AMFEFVSAIA NKLSTVVKGV GKIEHQFWRS FSNDRKTEPC
QSFVDGDLVE SFLDLSPEDM QRVANGLTIQ TADGTRPAMV EDVLKTVEEL SRIH
//