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Database: UniProt
Entry: A7S0J1_NEMVE
LinkDB: A7S0J1_NEMVE
Original site: A7S0J1_NEMVE 
ID   A7S0J1_NEMVE            Unreviewed;      1157 AA.
AC   A7S0J1;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   24-JAN-2024, entry version 79.
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=NEMVEDRAFT_v1g241997 {ECO:0000313|EMBL:EDO42742.1};
OS   Nematostella vectensis (Starlet sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Edwardsiidae; Nematostella.
OX   NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO42742.1, ECO:0000313|Proteomes:UP000001593};
RN   [1] {ECO:0000313|EMBL:EDO42742.1, ECO:0000313|Proteomes:UP000001593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX   PubMed=17615350; DOI=10.1126/science.1139158;
RA   Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA   Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA   Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA   Technau U., Martindale M.Q., Rokhsar D.S.;
RT   "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT   genomic organization.";
RL   Science 317:86-94(2007).
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}.
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DR   EMBL; DS469561; EDO42742.1; -; Genomic_DNA.
DR   RefSeq; XP_001634805.1; XM_001634755.1.
DR   AlphaFoldDB; A7S0J1; -.
DR   STRING; 45351.A7S0J1; -.
DR   EnsemblMetazoa; EDO42742; EDO42742; NEMVEDRAFT_v1g241997.
DR   eggNOG; KOG1897; Eukaryota.
DR   HOGENOM; CLU_002893_0_1_1; -.
DR   InParanoid; A7S0J1; -.
DR   OMA; HQDFLMR; -.
DR   PhylomeDB; A7S0J1; -.
DR   Proteomes; UP000001593; 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:UP000001593}.
FT   DOMAIN          75..552
FT                   /note="Cleavage/polyadenylation specificity factor A
FT                   subunit N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10433"
FT   DOMAIN          803..1117
FT                   /note="Cleavage/polyadenylation specificity factor A
FT                   subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03178"
FT   REGION          765..789
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1157 AA;  127514 MW;  9C92A432B940D3C0 CRC64;
     MTHNYVVTAQ KPTAVNAAVV GNFTGPDDLN LVIAKNTRLE IHLVTPEGLR PMLDVGLYGS
     VGVMELFRPP NEPQDLLFIL TAKYRVCILG YRKETGDIVT RACGDVQDRI GRPSDTGQIG
     IIDPSCRVIG LRLYDGLFKV IPLELDSDKE LKAFNIRLEE LHVVDIQFLY GCANPTIVFI
     YQDPHGRHVK TYEINLRDHE FAKGPWKQDN VEVEACRVIA VPNPLGGALI IGQESITYHK
     GSNYHAIAPP ALKQSSLTCH GKIDTNGSRY LLGDMNGRLY MLLLERQELI DGTYEVKDLK
     LEMLGETSIA HCLVYLDNGV VFIGSMLGDS QLAKLSTEPD ADGSYVQVME TFTNLGPIVD
     MVVVDLERQG QGQLVTCSGA KKEGSLRIIR NGIGIHEHAT IDLAGIMGIW ALKLRKTQQE
     YDDTLVLSFV GQSRRVLCTI HSRVLSLSGE EVEETEIPGF SDDQQTYYSG NVTGAQLIQV
     TAASVRLVNC ETRQLVSEWK HPSAKNISVA SCNTEQVVAA VGSELYYIEI MPGELRQISQ
     VTLEYEVACL DITPTVEGKS RADMVAVGLW TDISVRVLQL PKLNQLHVQM LGGEIIPRSI
     LKTAFEGIHY LLCALGDGTL FYFTMDPSTG ALAECKKVTL GTQPTMLRTF KSLSTVNVFA
     CSDRPTVIYS SNHKLVFSNV NLKEVNFMCP LNSQGYPDSL ALANDGSLTI GTIDEIQKLH
     IRTVPLGESP RRIAYQEATQ TFGVISVRIE ISEPGTSGTV PLHPSASTTA HNVSSSVGTG
     VSGSASSSAP DGITFGDEME IGSLLIIDQH TFEVTHAHQL HDNEQATSLM SCTLSDDPHT
     YYCVGTAYVF PEEPEPKAGR LLLFHLSEGK LVQVAEKEVK GAVYSLVEFN GKVLAGINST
     VSIFEWTADK EFRYECSYYD NILALYLKTK GDFILVGDLM RSMTLLVYLP LEGSFQEIAH
     DFSPKWMTAI EILDDDTFLG AENSYNLFTC TKDSGATTDE ERYHLQDAGQ YHLGEFVNVF
     RHGSLVMEHP GDASTPFQGC VLFGTVNGRI GIVAQIAQDL FNFLIQVQKK LNKVIKSVGK
     IDHSLYPFPH CSNLSHSRKM EPAHGFIDGD LIESFLDLPR ARMEEVVTGL QIDDGGMKKE
     CTVDDLVKTV EELTRIH
//
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