ID A0A2K6L717_RHIBE Unreviewed; 1140 AA.
AC A0A2K6L717;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 33.
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 Name=DDB1 {ECO:0000313|Ensembl:ENSRBIP00000019339.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000019339.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000019339.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000019339.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 RefSeq; XP_017733948.1; XM_017878459.1.
DR AlphaFoldDB; A0A2K6L717; -.
DR SMR; A0A2K6L717; -.
DR STRING; 61621.ENSRBIP00000019339; -.
DR Ensembl; ENSRBIT00000043211.1; ENSRBIP00000019339.1; ENSRBIG00000033611.1.
DR GeneID; 108533616; -.
DR KEGG; rbb:108533616; -.
DR CTD; 1642; -.
DR GeneTree; ENSGT00950000183151; -.
DR OMA; HQDFLMR; -.
DR OrthoDB; 226997at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000233180; Unplaced.
DR GO; GO:0031464; C:Cul4A-RING E3 ubiquitin ligase complex; IEA:Ensembl.
DR GO; GO:0031465; C:Cul4B-RING E3 ubiquitin ligase complex; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0097602; F:cullin family protein binding; IEA:Ensembl.
DR GO; GO:0003684; F:damaged DNA binding; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0160072; F:ubiquitin ligase complex scaffold activity; IEA:Ensembl.
DR GO; GO:0071987; F:WD40-repeat domain binding; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0051702; P:biological process involved in interaction with symbiont; IEA:Ensembl.
DR GO; GO:0035234; P:ectopic germ cell programmed cell death; IEA:Ensembl.
DR GO; GO:0044725; P:epigenetic programming in the zygotic pronuclei; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0051093; P:negative regulation of developmental process; IEA:Ensembl.
DR GO; GO:2000242; P:negative regulation of reproductive process; IEA:Ensembl.
DR GO; GO:0046726; P:positive regulation by virus of viral protein levels in host cell; IEA:Ensembl.
DR GO; GO:0045722; P:positive regulation of gluconeogenesis; IEA:Ensembl.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:0045070; P:positive regulation of viral genome replication; IEA:Ensembl.
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 GO; GO:0042752; P:regulation of circadian rhythm; IEA:Ensembl.
DR GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; IEA:Ensembl.
DR GO; GO:0007056; P:spindle assembly involved in female meiosis; IEA:Ensembl.
DR GO; GO:0070914; P:UV-damage excision repair; IEA:Ensembl.
DR GO; GO:0019076; P:viral release from host cell; IEA:Ensembl.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:Ensembl.
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 InterPro; IPR036322; WD40_repeat_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; SSF50978; WD40 repeat-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:UP000233180}.
FT DOMAIN 75..543
FT /note="Cleavage/polyadenylation specificity factor A
FT subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10433"
FT DOMAIN 790..1099
FT /note="Cleavage/polyadenylation specificity factor A
FT subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03178"
SQ SEQUENCE 1140 AA; 126968 MW; 74D082023E3D846D CRC64;
MSYNYVVTAQ KPTAVNGCVT GHFTSAEDLN LLIAKNTRLE IYVVTAEGLR PVKEVGMYGK
IAVMELFRPK GESKDLLFIL TAKYNACILE YKQSGESIDI ITRAHGNVQD RIGRPSETGI
IGIIDPECRM IGLRLYDGLF KVIPLDRDNK ELKAFNIRLE ELHVIDVKFL YGCQAPTICF
VYQDPQGRHV KTYEVSLREK EFNKGPWKQE NVEAEASMVI AVPEPFGGAI IIGQESITYH
NGDKYLAIAP PIIKQSTIVC HNRVDPNGSR YLLGDMEGRL FMLLLEKEEQ MDGTVTLKDL
RVELLGETSI AECLTYLDNG VVFVGSRLGD SQLVKLNVDS NEQGSYVVAM ETFTNLGPIV
DMCVVDLERQ GQGQLVTCSG AFKEGSLRII RNGIGIHEHA SIDLPGIKGL WPLRSDPNRE
TDDTLVLSFV GQTRVLMLNG EEVEETELMG FVDDQQTFFC GNVAHQQLIQ ITSASVRLVS
QEPKALVSEW KEPQAKNISV ASCNSSQVVV AVGRALYYLQ IHPQELRQIS HTEMEHEVAC
LDITPLGDSN GLSPLCAIGL WTDISARILK LPSFELLHKE MLGGEIIPRS ILMTTFESSH
YLLCALGDGA LFYFGLNIET GLLSDRKKVT LGTQPTVLRT FRSLSTTNVF ACSDRPTVIY
SSNHKLVFSN VNLKEVNYMC PLNSDGYPDS LALANNSTLT IGTIDEIQKL HIRTVPLYES
PRKICYQEVS QCFGVLSSRI EVQDTSGGTT ALRPSASTQA LSSSVSSSKL FSSSTAPHET
SFGEEVEVHN LLIIDQHTFE VLHAHQFLQN EYALSLVSCK LGKDPNTYFI VGTAMVYPEE
AEPKQGRIVV FQYSDGKLQT VAEKEVKGAV YSMVEFNGKL LASINSTVRL YEWTTEKELR
TECNHYNNIM ALYLKTKGDF ILVGDLMRSV LLLAYKPMEG NFEEIARDFN PNWMSAVEIL
DDDNFLGAEN AFNLFVCQKD SAATTDEERQ HLQEVGLFHL GEFVNVFCHG SLVMQNLGET
STPTQGSVLF GTVNGMIGLV TSLSESWYNL LLDMQNRLNK VIKSVGKIEH SFWRSFHTER
KTEPATGFID GDLIESFLDI SRPKMQEVVA NLQYDDGSGM KREATADDLI KVVEELTRIH
//