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Database: UniProt
Entry: A0A068Y6D7_ECHMU
LinkDB: A0A068Y6D7_ECHMU
Original site: A0A068Y6D7_ECHMU 
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}.
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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
//
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