ID A0A0V0TB48_9BILA Unreviewed; 1830 AA.
AC A0A0V0TB48;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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};
DE Flags: Fragment;
GN Name=DDB1 {ECO:0000313|EMBL:KRX36255.1};
GN ORFNames=T05_10580 {ECO:0000313|EMBL:KRX36255.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX36255.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX36255.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX36255.1};
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:KRX36255.1}.
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DR EMBL; JYDJ01000377; KRX36255.1; -; Genomic_DNA.
DR STRING; 144512.A0A0V0TB48; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000055048; 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:UP000055048}.
FT DOMAIN 745..1214
FT /note="Cleavage/polyadenylation specificity factor A
FT subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10433"
FT DOMAIN 1471..1785
FT /note="Cleavage/polyadenylation specificity factor A
FT subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03178"
FT NON_TER 1830
FT /evidence="ECO:0000313|EMBL:KRX36255.1"
SQ SEQUENCE 1830 AA; 205786 MW; 124DEB6856576161 CRC64;
MEGHENNDGT DNFTRKLKIL KDVHDFIYDD HDEDRKREAF LDDELFLHFR LRVKSFAVRD
SMLTSCHSFN PWILARFGFR YADKVVSCSD CGYCIDEVCC KNMMDDSNRK AAIKKMVDFH
GKSCIFKNNP VPGLFCAPEI LTFKEILRHL NRQFSILQPI SYRIEKMQFS DFDSIVPQQD
LYLLKDFLSK RRGINEGEAN AILSKLDNVV SAKLLLVALF GWTAFKRSLR DADDEKLECI
YCCGSFYPAA FSSSSLVSSQ QTDQVVFNPA TEHYYWCPIV RSKTIKILPS RISVKTCVPY
WRYLVSACLR TFSINDLSGI LYTDDYADKY SVDAIIVAEQ SASCEVFGVY SFEVSLMNLR
LSWKRVFHVP VRNYVRIPHW EYHIRFSPED GRKVPCTDVL NRFKRLNTGM WIRRYMKDEP
WLTNSLAHKT CTPLECQILE KMVSRFWQRP KYYVDDPYEP YNQRYGISES LPKILNAHVK
RPKILMDEST ERQSYRNSII FRFDQIQKKS GGNKYGRLQY LNQLVTEFQN SESNDAKRQI
VANLANFAYD PVNHEFLTTL RVHILFSDCL NEADPSMVEF ALGGLCNMIQ QPICRRFVLE
NLSEKVVSLL NSSNVETVVS ALTVLIFLLH DPKIKNAEII AKVQMLAEQN NQVRIANLAK
LFIRHLHSTM SNYIVTAKAA TAVTHSLHGS FTAPGSSDLI VFKNSRFEVH SVSAEGLQYL
TEGKMFGRIG AAKLFTPKGE NKALMVIVTL KQDVAIVEYD NGRIKTLASR NISENFGRPA
SNGILLSVHP DGEIIGLRIM SSTFKCITWN RATSKLSTYS LNYSLTHLSD FVFLHGFQFP
MIALIYGDLV GRHVITCRIS LDEQEFENGP WSRGHIEWEA HTLIAVPPPL CGVIVVGCSS
LLYIKDNSTI STVSPPFLSK SIVNCYDAAP DGLTYFLGQL DGTLSLLKLD IETDAEGKVT
LSRMRASILG VTSPPDSLSY MHKESLLFVG SRIADSKLLR LNSLAICDET WTEVESFPNL
APIVDMVLVD MAKQGQGEII SCSGYGKDGS LKVIRSGIGL YELARLDIPF VNRVWALRYI
TNEPYDNLFI LGVVGNSTMV IKFQENQAEQ ISVDGLETAE QTFVAANCHM TDGALAIVQV
VRSKIQLADA SLDGRKLDEW KFPDGSEVSL AACEGTSGRL LVACRHILHY FNVRDDRLQL
VTTRTMENEA SCVEFGCLSD EGVGVCIVGH WTKICLQLLF VPSLEPVQTV YLEDSSVIRS
ALMCKFESNM YLFVSLADGN LIFYSIDENS FALIDGKKVS LGTDSISLKM FKTKNTLSIL
ACTEKPTVIY MNNNKLQFSS LDSSAIYYMT PLFTSAYDNG VLFTNGQCLT IGIVDEIKKL
HIRSVVLGET PRRIVWQPEN KLVGVLTIRI MDLPGNSSSE SSASNRALHS ASAPPLRRAT
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 GSILIYCQIQ DSHFRVLNDL
QRCFSDIVPD NVGCIAYDSY RRYVVYEKNA PAFGFIDGDL IEQLLEMPRQ EAIRLINGWI
AAGRISPERC SNITTAQHII DLIEELSRIH
//
