ID A0A0V0RN31_9BILA Unreviewed; 1790 AA.
AC A0A0V0RN31;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=mrpl-35 {ECO:0000313|EMBL:KRX15738.1};
GN ORFNames=T07_10061 {ECO:0000313|EMBL:KRX15738.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX15738.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX15738.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX15738.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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|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:KRX15738.1}.
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DR EMBL; JYDL01000124; KRX15738.1; -; Genomic_DNA.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000054630; 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 GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.150.910; -; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
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.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF101908; Putative isomerase YbhE; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU368023};
KW Nucleus {ECO:0000256|RuleBase:RU368023};
KW Reference proteome {ECO:0000313|Proteomes:UP000054630}.
FT DOMAIN 705..1174
FT /note="Cleavage/polyadenylation specificity factor A
FT subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10433"
FT DOMAIN 1431..1745
FT /note="Cleavage/polyadenylation specificity factor A
FT subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03178"
FT REGION 1376..1400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1790 AA; 200813 MW; E8BF06426F678EC4 CRC64;
MEGHENNDGT DNFTRKLKIL KDVHDFIYDD HDEDRKREAF LDDELFLHFR LRVKSFADSM
LTSCYSFNPW ILARFGFRYA DKVVSCSDCG YCIDEVCSKN MMDDSNRKAA IKKMIDFHGK
SCIFKNNPVP GLFCAPEILT FKEILRHLNR QFSILQPISY RIEKMQFSDF DSIGINEGEA
NAILSKLDNV VSAKLLLVAL FGWTAFKRSL RDADDEKLEC IYCCGSFYPA AFSSSSLVSS
QQTDQVVFNP ATEHYYWCPI VRSKTIKILP SRISVKTCVP YWRYLVSACL RTFSINDLSG
ILYTDDYADK YSVDAIIVAE QSASCEIFGV YSVFHVPVRN YVRIPHWEYH IRFSPEDGRK
VPCTDVLNRF KRLNTGMWIR RYMKDEPWLT NSLAHKTCTP LECQILEKMV SRFWQRPKYY
VDDPYEPYNQ RYGISESLPK ILNAHVKRPK ILMDESTERQ KSGGNKYGRL QYLNQLVTEF
QNSETNDAKR QIVANLANFA YDPVNHEFLT TLRVHILFSD CLNETDPSMV EFALGGLCNM
IQQPICRRFV LENLSEKVVS LLNSSNVETV VSALTVLIFL LHDPKIKNAE IIAKVQMLAE
QNNQVRIANL AKLFIRRAKD LAQLHLHSTM SNYIVTAKAA TAVTHSLHGS FTAPGSSDLI
IFKNSRFEVH SVSAEGLQYV TEGKMFGRIG AAKLFTPKGE NKALMVIVTL KQDVAIVEYD
NGRIKTLASR NISENFGRPA SNGILLSVHP DGEVIGLRIM SSTFKCITWN RATSKLSTYS
LNYSLTHLSD FVFLHGFQFP MIALIYGDLV GRHVVTCRIS LDEQEFENGP WSRGHIEWEA
HTLIAVPPPL CGVIVVGCSS LLYIKDNSTI STVSPPFLSK SIVNCYDAAP DGLTYFLGQL
DGTLSLLKLD IETDAEGKVT LSRMRATILG VTSPPDSLSY MHKESLLFVG SRIADSKLLR
LNSLAICDET WTEVESFPNL APIVDMVLVD MAKQGQGEII SCSGYGKDGS LKVIRSGIGL
YELARLDIPF VNRVWALRYI TNEPYDNLFI LGVVGNSTMV IKFQENQAEQ ISVDGLETAE
QTFVAANCHM TDGALAIVQV VRSKIQLADA SLDGRKLDEW KFSDGSEVSL AACEGTSGRL
LVACRHILHY FNVRDDRLQL VTTRTMENEA SCVEFGCLSD EGVGVCIVGH WTKICLQLLF
VPSLEPVQTV YLEDSSVIRS ALMCKFESNM YLFVSLADGN LIFYSIDENS FALIDGKKVS
LGTDSISLKM FRTKNTLSIL ACTEKPTVIY MNNNKLQFSS LDSSAIYYMT PLFTSAYDNG
VLFTNGQCLT IGVVDEIKKL HIRSVVLGET PRRIVWQPEN KLVGVLTIRI MDLPGNSSSE
SSASNRALHS ASAPPLRRTT LTVDPNSAIN EGAVNIGAED TGVDRSIETH SFLLLDQNSF
DVLHAYSMNP LEECTSILSC TMGEDQNPFF ILSAAVITAD ETEPLQGRLL MLRYERDGQG
NSSLNLVHEK EVNGCVYAMA SFKSKLLVAM NSSVLLFEWS DVTGLQLVSS CSLFVTAMHL
KVRDEVILVG DIQRSIAVLR YVPSESSFVE EARDYHPNWI SAIEVIDNDY FMAAENSLNI
TVSQKDLQQQ PVSESQVVKS AGRLHLGEYI NVFKHGALSM YSYAGISSLV SNPIMIGTAE
GSILIYCQIH DSHFRVLNDL QRCFSDIVPD NVGCIAYDSY RRYVVYEKNA PAFGFIDGDL
IEQLLEMPRQ EAIRLINGWI TAGRISPERC TNITTAQQII DLIEELSRIH
//
