ID A0A068Y6D7_ECHMU Unreviewed; 1332 AA.
AC A0A068Y6D7;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=EmuJ_000763400 {ECO:0000313|EMBL:CDS40072.1};
OS Echinococcus multilocularis (Fox tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX NCBI_TaxID=6211 {ECO:0000313|EMBL:CDS40072.1};
RN [1] {ECO:0000313|EMBL:CDS40072.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23485966; DOI=10.1038/nature12031;
RA Tsai I.J., Zarowiecki M., Holroyd N., Garciarrubio A., Sanchez-Flores A.,
RA Brooks K.L., Tracey A., Bobes R.J., Fragoso G., Sciutto E., Aslett M.,
RA Beasley H., Bennett H.M., Cai J., Camicia F., Clark R., Cucher M.,
RA De Silva N., Day T.A., Deplazes P., Estrada K., Fernandez C., Holland P.W.,
RA Hou J., Hu S., Huckvale T., Hung S.S., Kamenetzky L., Keane J.A., Kiss F.,
RA Koziol U., Lambert O., Liu K., Luo X., Luo Y., Macchiaroli N., Nichol S.,
RA Paps J., Parkinson J., Pouchkina-Stantcheva N., Riddiford N., Rosenzvit M.,
RA Salinas G., Wasmuth J.D., Zamanian M., Zheng Y., Cai X., Soberon X.,
RA Olson P.D., Laclette J.P., Brehm K., Berriman M., Garciarrubio A.,
RA Bobes R.J., Fragoso G., Sanchez-Flores A., Estrada K., Cevallos M.A.,
RA Morett E., Gonzalez V., Portillo T., Ochoa-Leyva A., Jose M.V., Sciutto E.,
RA Landa A., Jimenez L., Valdes V., Carrero J.C., Larralde C.,
RA Morales-Montor J., Limon-Lason J., Soberon X., Laclette J.P.;
RT "The genomes of four tapeworm species reveal adaptations to parasitism.";
RL Nature 496:57-63(2013).
RN [2] {ECO:0000313|EMBL:CDS40072.1}
RP NUCLEOTIDE SEQUENCE.
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) 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|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; LN902841; CDS40072.1; -; Genomic_DNA.
DR STRING; 6211.A0A068Y6D7; -.
DR eggNOG; KOG1897; Eukaryota.
DR OMA; HQDFLMR; -.
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.
DR SUPFAM; SSF69322; Tricorn protease domain 2; 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}.
FT DOMAIN 75..578
FT /note="Cleavage/polyadenylation specificity factor A
FT subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10433"
FT DOMAIN 876..1277
FT /note="Cleavage/polyadenylation specificity factor A
FT subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03178"
FT REGION 842..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1087..1161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1332 AA; 146361 MW; 027AC1CAEA0393EA CRC64;
MSQFYHVTTQ RSTSVTKALT GNFTGPNDLN LLIIKNSYLE LYDVTSEGLK LIHDVPLNAS
VLTALFFRQK LWRRDFLFIL THKADIAIIE CIRKNDSIEF VTIMSASIAD SAARMLDQGF
DALVDPGATY IVIRMYYGML KLIPIANLSG PRDPLNKVDQ QAMPISVRIE ETQIVDMVFL
HGYATPTFAL IYEDDMVASI KMYDISGKDP ILRSVPVNVD SIETSSKILI PVPAPYNGFI
LVGDSIICYH TRETFHISQY IPQAQNSRIV CYAKVDSRRY LLGDIAGRLY MVHLLPQDEK
TIRPIPSTSR DMTHASPRIG SIRIELLGET AIPESIVYLD NGVVFIGSYL GDSQLIQLNP
EIDPDKNSYI TILEEFTNIG PIVDMVFFEN DGQSQLITCS GCYKEGSLRV IRNGIGIQER
ATIDRVDIKG VWCFPLKSDT YDDSIIVSLI NRSQLACITE DCLASLTLEG FILAEQTLHC
DVVYPSGYKQ NPRSLLLQAT TYGLRLIGIQ GLMGRGCLAK WRSPTDRSVS SLASRGDYVA
VASGSDLFAL RITGTPEAPQ FTQIGNAALP HEVACVDLTP FDRSVAAKAA IYSSAFQSPV
SSVKPSVRIG NNEEEAMDSS NSGDPLDDLE PEYVVVGMWM GHGVALLKLP SLEVVCIEPL
PTMTPTSGIA ILPRSITIAQ FEGLTYLFTV TGDGSLYYYN LDCSTEKIVI REAKRLSAGT
GPQMRLTQWR SHGKRNVFVC SNRPCIVYSN RHKLVFSNVN IKEVSFMSPL NGFHYKDCIC
MVTPSGLMIG SVDNLQKLHV RRIPLNETPR RLALQSATNS LGVISCRREV FQEGTGFKPI
RTSASLSPKV PRSYSSTPKS PASSSNPEKC TDIEASSLLI YNQSTMDLQF VHTFHYSQVV
VETAMSVGSV DLGNDAGVLY AVGTALIVKG EHDPKKGRIH LLRWNPVALS LESVLTYDVP
GTVFRVIEFN GRILAAIGSS VRLFEFCGDT LRQDSTFNDN IMSLYLRTKG DYVLIGDLMR
SLCLLLYKPN RSNFEVIGRH HCPRYTSGIE IIDDEHFLSG DADGNIHVLG RNLPGNTDEP
VVPSLRVTEA ATSPTPVTVS VSTPKPMADT PDVAGPCDAA DNSSASTSTS APETAPAQDS
EEQSGVSLQA PTPQSIDLPR CPSSDGKALV DCAYMHTGES INVFVRGNMN TLGVDRWSAI
GETHTMYGTA QGCLGLVAHL SPILFAFLKE VESRLSRLIV PVGNFSQESW RSCKDCLWTV
RVAHNIIDGE LIESFLDLSL DDKNKVVQGL KIPASMEDFG TAGLSKFNEN VETKDCTVND
LMRVVEELAA LH
//