ID A0A182QID4_9DIPT Unreviewed; 1138 AA.
AC A0A182QID4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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};
OS Anopheles farauti.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=69004 {ECO:0000313|EnsemblMetazoa:AFAF010772-PA, ECO:0000313|Proteomes:UP000075886};
RN [1] {ECO:0000313|Proteomes:UP000075886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FAR1 {ECO:0000313|Proteomes:UP000075886};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles farauti FAR1 (V2).";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AFAF010772-PA}
RP IDENTIFICATION.
RC STRAIN=FAR1 {ECO:0000313|EnsemblMetazoa:AFAF010772-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- FUNCTION: Plays a role in DNA repair. May be a component of an E3
CC ubiquitin-protein ligase which promotes histone ubiquitination in
CC response to UV irradiation. Histone ubiquitination may be important for
CC subsequent DNA repair. {ECO:0000256|RuleBase:RU368023}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|RuleBase:RU368023}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU368023}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123, 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; AXCN02000116; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A182QID4; -.
DR STRING; 69004.A0A182QID4; -.
DR EnsemblMetazoa; AFAF010772-RA; AFAF010772-PA; AFAF010772.
DR VEuPathDB; VectorBase:AFAF010772; -.
DR OrthoDB; 226997at2759; -.
DR Proteomes; UP000075886; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; 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 Cytoplasm {ECO:0000256|RuleBase:RU368023};
KW Nucleus {ECO:0000256|RuleBase:RU368023}.
FT DOMAIN 75..544
FT /note="Cleavage/polyadenylation specificity factor A
FT subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10433"
FT DOMAIN 789..1098
FT /note="Cleavage/polyadenylation specificity factor A
FT subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03178"
FT REGION 748..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1138 AA; 126176 MW; B5DC918523BF4680 CRC64;
MAHNYIVTAQ KPTAVTACVT GNFTSPTDLN LIVAKSSRLE IYLVTPEGLR PIKEVGINGK
IAVMKLFRPA EETKDLIFIL TQRYNAMILQ CAVQGDDIEI ITKAHGNVAD RVGKPAETGI
LAVIDPKARV IGMRLYEGLF KIIPLDKDTN ELKATSLRME EMHVQDVEFL YGTTHPTLIV
IHQDINGRHI KTHEISLKDK EFTKIAWKQD NVETEATMLI AVPMPLGGAI VIGQESIVYH
DGDSYVAVAP AIIKQSTINC YARIDSKGLR YLLGNMAGNL FMMFLETEEN AKGQTTVRDI
KVELLGEITI PECITYLDNG VLFIGSRHGD SQLVKLNTTA GENGAYVMLM ETFTNLAPIV
DICVVDLERQ GQGQMITCSG SFKEGSLRII RNGIGIQEHA CIDLPGIKGM WALRVGIDDS
PYDNTLILSF VGHTRVLMLS GDEVEETEIA GFVGDQQTFY CANVSHGQIL QVTPTSARLI
SCDNKSLICE WKPPEGKRIG VVSANTTQIV CASAQDVYYI EIENGKLEFK GQTTLSYEVA
CLDVSPLEDS GTRSEFVAVG LWTDISACVL KVPTLELLHK EKLGGEIIPR SILMAAFEGI
NYLLCALGDG SMYYFVLNKA TGGLSDQKKV TLGTQPTILK TFRSLSTTNV FACSDRPTVI
YSSNHKLVFS NVNLKEVNHM CSLNAEAYQD SLALATRNSV IFGTIDEIQK LHIRTVPLGE
SPRRIAYQES SQTFGVVTFR MDVQDSSGLT PARQSASTQT NNITQSSSMG MLKPGASSTE
FGQEVEVHNL LIIDQNTFEV LHAHQFMQTE YALSLMSARL GNDPNTYFVV GTGFVNPEDP
EPKIGRIIIY RYADNELKLV SEKEIKGACY SLVEFNGRVL ACINSTVRLY EWTDDKDLRL
ECSHFNNVLA LFCKTKGDFI LVGDLMRSIT LLQYKQMEGS FEEIARDYQP KWMTAVEILD
DDAFLGADNS NNLFVCLKDG AATTDEERQQ MPEVAQFHLG DMVNVFRHGS LVMQNISERT
TPTTGCVLFG TVSGAIGLVT QIQSDFYEFL HKLQENLTNT IKSVGKIDHA YWRSYHTEMK
TERCGGFIDG DLVESFLDLS REKMREAAFG LEIDVEGTKR EATVDDIIKI VEDLTRIH
//
