ID A0A267GIJ9_9PLAT Unreviewed; 1258 AA.
AC A0A267GIJ9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-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};
DE Flags: Fragment;
GN ORFNames=BOX15_Mlig015655g2 {ECO:0000313|EMBL:PAA85826.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA85826.1, ECO:0000313|Proteomes:UP000215902};
RN [1] {ECO:0000313|EMBL:PAA85826.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA85826.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA85826.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) 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|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:PAA85826.1}.
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DR EMBL; NIVC01000303; PAA85826.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A267GIJ9; -.
DR STRING; 282301.A0A267GIJ9; -.
DR Proteomes; UP000215902; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|RuleBase:RU368023};
KW DNA repair {ECO:0000256|RuleBase:RU368023};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleus {ECO:0000256|RuleBase:RU368023};
KW Reference proteome {ECO:0000313|Proteomes:UP000215902};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 37..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 162..620
FT /note="Cleavage/polyadenylation specificity factor A
FT subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10433"
FT DOMAIN 898..1210
FT /note="Cleavage/polyadenylation specificity factor A
FT subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03178"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PAA85826.1"
SQ SEQUENCE 1258 AA; 136566 MW; 28801F08A1D3A3F6 CRC64;
CVSESVGAEA LHLFVFVVCS SFQRVVQRSK GRTYRKFALF ILSLLSAIIM SKNYIVTAQR
STAVSCSLTG HFTGNNYRNL LVAKHNTLEL HVVSSSGVKT IKEISIYGKI SVLLGFQPQG
RTSGTDLIFL LTQKKDAMIL ECQVDNAGSL AMEATEAAGD YLADNSHCLK VVTLASGNLH
ERIGRQSENG PLGIVDPRGR VVALQLYEGL LKVIPVSFVQ KPYNPEAGSD TLKAFNVRIE
EIDLVDMTFI DGVNPTIAYI TQDSVGRHLK TVEINCDTRD LAPGPWKIDS IQAQASMLIP
LPMPHPGLLI VGQETVTIRS KDGSLKTIAP PVIRTSPMLA FDRLDCNRFL LGDMAGRLFM
LFLEREGDRV KDMKVELLGE ISIPETISYL DNNVVFIGSR FGDSQLIRLL VEADSSGNFV
SVLESFVNIA PVVDMAVVDI DNLGQGQLVT CSGAFKDGSL RIIRSGVGIN EMVNIDLAGI
KGVWNLRTAG SSFDNFIIIT FQNQTKTLLM SCSPCDPAME IEEVPMPAFE TAERTYLCQN
VLGGQIVQVT PQSARLLDST GKRRLAEWLP PSGRTVSVCG AGQRHLLIAI GRQLTCLAIG
EGTLTVLAER ELPNEVACID ATPLPDGFDD GGGIVAVGLW VEISVRLLRL RNLEEVCVEP
LGVQIIPRSI VLATMPCGVY LFVGIGDGTM VYFTVVPGPA LVNRKHVIIG TQPMGLCWLP
SQSLFVCTDR PAIAHCVSGK LVISHVNTRQ VNYVCPILLS AASIDAQQPQ QCICLVTNSQ
LLFGTIDDMQ KLHIRTVPLG ESARKVAHQP ESGTLAVVTS RVDLRHEGGY APARTSVSVT
APIQLTPDGA ATAAGKRHHA HASGMVGAAA TVASAAAAAA VAAASSAEVD EELEVTSVVV
LEQNSLQPLC SMQFPSNPSC VETATSITSG QFGTDCATYF VVGTCYIRPN ESEPSAGRLL
MLQYTADSPY LTKVAEKEIR GAPYSMCCFN QRLLVCVNSS VRLFEWSENE RELRLECSHF
NNIIALYLKT KGDFALVGDL LRSMSLLLYK PVETSLEEIV RDHAPNWMLA IEIIDDDAFL
GAENCGNLFV CSRESENSGG EERPRLQENA WYHLGDTVNT FQHGSLVMSQ LGERLVTVST
PILFATQSGA VGLICQLPPP LFEFLNELQR RLASLIVGVG GVEHAKYRSF ETEHRTEPAK
DFIDGDLLEA ALDLGRDKLE TVAQGLTRKT DFSSAVSDSV PCTVEDLIRI LEELSRLH
//
