ID A0A369S5S1_9METZ Unreviewed; 1133 AA.
AC A0A369S5S1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, 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=TrispH2_006337 {ECO:0000313|EMBL:RDD41784.1};
OS Trichoplax sp. H2.
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=287889 {ECO:0000313|EMBL:RDD41784.1, ECO:0000313|Proteomes:UP000253843};
RN [1] {ECO:0000313|EMBL:RDD41784.1, ECO:0000313|Proteomes:UP000253843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Panama {ECO:0000313|EMBL:RDD41784.1,
RC ECO:0000313|Proteomes:UP000253843};
RC TISSUE=Whole clonal animals {ECO:0000313|EMBL:RDD41784.1};
RX PubMed=30042472; DOI=10.1038/s41598-018-29400-y;
RA Kamm K., Osigus H.J., Stadler P.F., DeSalle R., Schierwater B.;
RT "Trichoplax genomes reveal profound admixture and suggest stable wild
RT populations without bisexual reproduction.";
RL Sci. Rep. 8:11168-11168(2018).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDD41784.1}.
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; NOWV01000067; RDD41784.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369S5S1; -.
DR STRING; 287889.A0A369S5S1; -.
DR Proteomes; UP000253843; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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; 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:UP000253843}.
FT DOMAIN 75..543
FT /note="Cleavage/polyadenylation specificity factor A
FT subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10433"
FT DOMAIN 786..1093
FT /note="Cleavage/polyadenylation specificity factor A
FT subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03178"
SQ SEQUENCE 1133 AA; 125729 MW; 5181EF613D50DDCE CRC64;
MACNYVVTAH KPTAANASLF GNFTGPHDLN LIVAKNNRLD IQLVTAEGLV PLLDVGVYGR
IASMQLIRPE NENCDLLFVL 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 IKLNTSPDSE TDSYIDVIDN FTNLGPIIDM
VSVDLDKQGQ SQLVTCSGFG KNASLRVLRN GIGIHELANI DLDHICGIWR LRTVSRSISE
YDDVLVLSFA GHSRFLKFDG REVEETDISG FDDYKETDFA ANVAFDQIVQ ISNESVRLAG
CDGRGLLQEW KPPNGKTISK STAGNTQIMV ASGCELFYLE IGEGELKQVS NISLEHDIAC
IDISLKDDNE RAQICAVGLW VDMSARLLLL PNLQLMLTES LGGDIIPRSI MLNRFDNEIY
LLVAMGDGTL AYYLVNTTTC SLTNRKSVNL GVVHSNLYTF KSGSISNVFA CSDRPTVIYI
NNHKLVFSNV NLKKVNFMSP FHSESFPNSL ALVNDSGFII GTIDEIQKLH IRTKPLGETT
RQEESQSFGI ITCRTEVPSE DDKNFVPTHQ SASLLVSNRT MCPEQSDNSS STFDSDTLSE
KNIDSVLIID QHSLDAQCAL QLQDCEWGMS LISCMFENDP EAYYCVGTAF VNLEDKEPTK
GNIRILKYFE GKIQQVHSKE VSGAVYCMVA FNGKLLASVN STVSVYEWTS NKELVEETSF
HNNVLALYLK TKGDFILIGD LMRSISLCAY RPMNNEIELI CKNNDPNWMT AVEIIDDDSY
LGGENSHNLF TCQKNSSSSE EEQKHLPTVG VYHVGEFVNV FRQGSLVMQN TVDIPDSVQG
SILFGTVSGA VGVVVTLAPA MFEFVSAIAN KLSTVVKGVG KIEHQFWRSF SNDRKTEPCQ
SFVDGDLVES FLDLSPEDMQ RVANGLTIQT ADGTRPAMVE DVLKTVEELS RIH
//
