ID A0A0S7DM82_9EURO Unreviewed; 920 AA.
AC A0A0S7DM82;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:GIM38301.1};
GN ORFNames=ALT_000683 {ECO:0000313|EMBL:GIM38301.1}, CNMCM8060_005725
GN {ECO:0000313|EMBL:KAF4177135.1};
OS Aspergillus lentulus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=293939 {ECO:0000313|EMBL:GIM38301.1};
RN [1] {ECO:0000313|EMBL:GIM38301.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM38301.1};
RA Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT lentulus IFM 54703T.";
RL Genome Announc. 4:e01568-15(2016).
RN [2] {ECO:0000313|EMBL:KAF4177135.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4177135.1};
RA dos Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E.,
RA Silva L.P., Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RT "Genomic and phenotypic heterogeneity of clinical isolates of the human
RT pathogens Aspergillus fumigatus, Aspergillus lentulus and Aspergillus
RT fumigatiaffinis.";
RL bioRxiv 0:0-0(2020).
RN [3] {ECO:0000313|EMBL:KAF4177135.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4177135.1};
RA Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E., Silva L.P.,
RA Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the XPC family. {ECO:0000256|ARBA:ARBA00009525}.
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:GIM38301.1}.
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DR EMBL; BCLY01000008; GIM38301.1; -; Genomic_DNA.
DR EMBL; JAAAPS010000035; KAF4177135.1; -; Genomic_DNA.
DR STRING; 293939.A0A0S7DM82; -.
DR VEuPathDB; FungiDB:TMP_alenIFM54703_3992; -.
DR OrthoDB; 181129at2759; -.
DR Proteomes; UP000713487; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR Gene3D; 2.20.20.110; Rad4, beta-hairpin domain BHD1; 1.
DR Gene3D; 3.30.60.290; Rad4, beta-hairpin domain BHD2; 1.
DR Gene3D; 3.30.70.2460; Rad4, beta-hairpin domain BHD3; 1.
DR Gene3D; 3.90.260.10; Transglutaminase-like; 1.
DR InterPro; IPR018327; BHD_2.
DR InterPro; IPR004583; DNA_repair_Rad4.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR018325; Rad4/PNGase_transGLS-fold.
DR InterPro; IPR018326; Rad4_beta-hairpin_dom1.
DR InterPro; IPR018328; Rad4_beta-hairpin_dom3.
DR InterPro; IPR042488; Rad4_BHD3_sf.
DR InterPro; IPR036985; Transglutaminase-like_sf.
DR PANTHER; PTHR12135:SF0; DNA REPAIR PROTEIN COMPLEMENTING XP-C CELLS; 1.
DR PANTHER; PTHR12135; DNA REPAIR PROTEIN XP-C / RAD4; 1.
DR Pfam; PF10403; BHD_1; 1.
DR Pfam; PF10404; BHD_2; 1.
DR Pfam; PF10405; BHD_3; 1.
DR Pfam; PF03835; Rad4; 1.
DR SMART; SM01030; BHD_1; 1.
DR SMART; SM01031; BHD_2; 1.
DR SMART; SM01032; BHD_3; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT DOMAIN 533..590
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01030"
FT DOMAIN 592..655
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01031"
FT DOMAIN 662..736
FT /note="Rad4 beta-hairpin"
FT /evidence="ECO:0000259|SMART:SM01032"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..892
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 920 AA; 103773 MW; E5C8F2A6B6E4F9F5 CRC64;
MPPFVPRKRV SSEDPPTAKR QNATPIVEIA DFEEDSDSDS SLSDAPSSLD DEPHEKRDLQ
KQKKQASDGS ESESESDDDD DEVDWEDAMD SKFTSASVSV TPAPAVQDLE LTLDKNEIHL
ADIADGKKGP SKIERQIRIA THCLHVQFLL YHNAVRNAWA NDIKVHEILR RKLPAGIHKE
VKRWRTASGL DPPEKKPEVK SKKKKGKTRK SDRDWSEGSS RVEPGKPDMS RGDPIISLLR
ILAAYWRKQF KITAPGLRKV GYRPMAHLEA EISSFQKDEH DPERHGERIR DIEEFRTAAE
RMEGSRDLGA QLFTALVRAL GIEARLVANL QPLGFGWTKA EAYTPRPKVE EGTIEQNGES
EPIVGLESDS SDSETAPAHK HKPKKYDKDL PFPIYWTEVA SPITHEVIPV DPLILSNPVA
TTPELQAAFE PRGAKAEKAK QVICYVVAYS SDKTAKDVTT RYLRRRTWPG KTKGYRIPVE
RIPLPGRKRK FFEYDWFRTI LRVYERCEKN RTKVDEVEDA TDLCPNQPEK KQVKEGDTLQ
SLRSSTEFVL ERFLRREEAL RPGAQPIRTF VSGKGDKAKE EKVYRRGDVL KCLSAESWHK
EGRQIKMGEA PLKLVPIRAV TLLRKREVDE IERETGEKPK QGLYAKYQTE YIIPPPIRDG
IIPKNEYGNI DCFVPSMVPR GAVHIPLPGT VRICKKLGID YAEAVTGFEF GSKMAVPVIQ
GVVVASENED LVKDAWRAED AEKRKKEQLK AEKRILQTWR KFLFGLRIAE RVREEYGADD
GDMERESQNP FASRQARSQV RPPPVPEAAH EWLGEPADRG GGFLLPGEDD GDDGDLVVED
HHPRQARPSV QQSEALSEDE DDQGPGHDAI SISSNGPADL SSPQQISDSE EDEPSASASD
YEPPSTRRRT RNPGRRTRGK
//
