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Database: UniProt
Entry: A0A2L2TL89_9HYPO
LinkDB: A0A2L2TL89_9HYPO
Original site: A0A2L2TL89_9HYPO 
ID   A0A2L2TL89_9HYPO        Unreviewed;      1161 AA.
AC   A0A2L2TL89;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=DNA damage-binding protein 1 {ECO:0000256|ARBA:ARBA00014577};
OS   Fusarium venenatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=56646 {ECO:0000313|EMBL:CEI68933.1, ECO:0000313|Proteomes:UP000245910};
RN   [1] {ECO:0000313|Proteomes:UP000245910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A3/5 {ECO:0000313|Proteomes:UP000245910};
RA   King R.;
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the DDB1 family.
CC       {ECO:0000256|ARBA:ARBA00007453}.
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DR   EMBL; LN649231; CEI68933.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2L2TL89; -.
DR   STRING; 56646.A0A2L2TL89; -.
DR   OrthoDB; 226997at2759; -.
DR   Proteomes; UP000245910; Chromosome iii.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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   Reference proteome {ECO:0000313|Proteomes:UP000245910}.
FT   DOMAIN          73..591
FT                   /note="Cleavage/polyadenylation specificity factor A
FT                   subunit N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10433"
FT   DOMAIN          804..1130
FT                   /note="Cleavage/polyadenylation specificity factor A
FT                   subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03178"
SQ   SEQUENCE   1161 AA;  128648 MW;  4376E88AB33F7105 CRC64;
     MAYVAPIHRA TSIRHALRAN VLDPEIDDLI VAKANRLEIW RLTEKGLVCQ QTKLIHGTIS
     MLQRLRPKGS ETDLLFVGTD RLQYFNLIWN DATKQLETIE RVIEDMSEPY MRQSQSQNKC
     LVDPTGRFLA MHLWEGVLNV FKLPTRKGST NKLEVLDQVR ITELFMKAST FTYSYTNHPT
     IAFLYKTQMD QEETRLVIYR LTHDDKGNTV SKFDPHKDRE LDVEIPDPYA SMLIPVPLDE
     EKRYHVRNKE GAKPHLGGLL VIGETLLTYY DGQTHRSVSA GLKDPRIFVA WAEYDSTRYL
     LADDYGRLDL LTIQTNLEPT GVVVTGMVLE PFEYGNSPAI TSRASSLVYL GDGTLFVASH
     HGDSQLYQID VETKTVMLVQ SFLNNAPILD FSIMDMGNRE GDTQAGNAFS SGQSRIVAGC
     GAYHDGTLRS IRSGVGLEDR GVLDELEGTR GLFTLHSYGS DMVDTLVVSS ITETRILSFD
     PEGGIEEVYS YQGMSLDSET LLASNLPSGQ LLQVTPKSVV LLDPEGGTTI SKWDVPSGKT
     ITRASANGKW ALLSVDGTSL VSLNLLQNLA VNAQQINDNA TSQPDQISCI HAARDPPDLG
     VVGWWSSGQI SLIDMASLKP LHGESMRQTE DSATVPRDVA LVQLHPPDIS GPTLLVAMED
     GNVVTFNVST KGFSVSGRKS VTLGSNPARL HILPQEDGTS NVFVTTEHAS LIYSSEGRVI
     FSATTADDAT FVAPFNSHAF PDSVVLSTDQ HIRICHVDRE RLTHVKSLPF NETVRRVAYS
     PGLKAFGLGS IRRELVNNEE VVTSSFRLVD EIVFKELGSP FPLNGSSTLE LVECVIRAEL
     PDVGGNPTER FIVGTSFISD GEVEDPNGTL GRILVLGVDA NRQVYQIVSH NLKGPCRCLG
     MIGDNIVAGL SKTVVVYSFS QETSSSGSLQ KLAAYRPAAI PIDIDVSGNM IGVGDLMQSL
     SLVEFIPAQD GNKAQLQERA RHFESLWTTA VCHIEGERWL EADSRGNLVV LQRNVDAPTE
     QDRRRLEITS EMGIGEQINR IRKLNVPAAE NNIVHPRAFL ASAEGSLYLY GDIAPQYQDL
     LMTFQSKMEE FVLALGNVEF KLWRSFRNDN RESEGPYRFI DGEMIERFLD MDEEQQELVC
     DGLGPTVEDM RNLIEELRRM H
//
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