ID   A0A0D2E6J6_9EURO        Unreviewed;      1096 AA.
AC   A0A0D2E6J6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIW51043.1};
GN   ORFNames=PV05_09800 {ECO:0000313|EMBL:KIW51043.1};
OS   Exophiala xenobiotica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW51043.1, ECO:0000313|Proteomes:UP000054342};
RN   [1] {ECO:0000313|EMBL:KIW51043.1, ECO:0000313|Proteomes:UP000054342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW51043.1,
RC   ECO:0000313|Proteomes:UP000054342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KN847322; KIW51043.1; -; Genomic_DNA.
DR   RefSeq; XP_013311627.1; XM_013456173.1.
DR   AlphaFoldDB; A0A0D2E6J6; -.
DR   STRING; 348802.A0A0D2E6J6; -.
DR   GeneID; 25331708; -.
DR   HOGENOM; CLU_000315_2_7_1; -.
DR   OrthoDB; 200191at2759; -.
DR   Proteomes; UP000054342; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd18008; DEXDc_SHPRH-like; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45626:SF51; SINGLE-STRANDED DNA-DEPENDENT ATPASE (EUROFUNG); 1.
DR   PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054342}.
FT   DOMAIN          468..655
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          927..1075
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          72..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..153
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1096 AA;  123310 MW;  A554491AE8A7E130 CRC64;
     MAANARMLLD PKSIKKNLKL GEDNQTKSAM RSQQEITQFP GHRGPPNHNP IQPQSSSRYL
     DHRALLDPRT LLNAKRSPGS TISPVPPSNQ DQDAHDGMPS MLRSSPALNR QHSGPRSLLE
     AVHGVESRVD HPRKKVKVNA SNDDAEPKRG RSYSHHPSSG IIGGYMRPDA ENSAENTLKS
     LVDLTNDEDD EVDDDVEFVS SRTLSGDEEV CYGHFSTNVH AHLIPKPKSN SVFQSDKEWP
     VMKCTLTRIP SKDTVIEVSD PFGIVFGRVN PDFAAALAPV LDGLEGIRTQ ARLVNRRKKP
     EEWPHLKCSE YLKMIVNVYG RRKDVQKVGK HFGQHNFWFR PPMAPEPGVP IVNPHGKKDV
     MPQPVRKTGQ GHVLSDARTL EEATEAVSKL FDSFANAAPA LVETEPPASI ITTPLLSHQK
     QALTFLMQHE HPRTFGDEES ENSSLWRRVI AKTGATVYRE VVSGISVRDE PDQVLGGLLA
     DVMGLGKTLE ALSLIAATLD DAMDFSREKV IRDDQNMLLA NTKATLVVCP TSTVKNWEDQ
     IATHIHPEKV SYYVYHGPNR ERNPYKLSKY DIILATYGVV ASEFSGRGSA GITPLKQLKW
     FRIILDEAHT IREHKALQSQ AIYSLEAQRR WCLTGTPIQN RLDDLGSLTR FLRLYPYDTP
     ARFNQYIRGP AQAGDPSFLK ALRVFVDSFT LRRLRDRIDL PERKDFVDLL DFSPDEKQLH
     DFFKEIAHVQ IQELAHMKQK NSGVQHHVLR GIMTLRLICA HGRDLLKEKD LAKLKGVTHS
     EAIDLDGDYK PSTISRQAAY ESLNLMTEAQ LDLCRRCERK ITQMEFEDDD GIRCYILPCF
     DLICAECFAA DKQTFDSMSD REVVTCPYCS KEIAAQYVGF SGSTTQEIIT APDDNIAQDE
     EDTEIHTYHG PHTKTKALLQ DIAAMVKDSE ALEAAGEAPL KCVVFSEFTS HLDLIEIALR
     DNGYSFVRID GTMSLNNRKK SLDALAYDND VIILLASIKA AGQGLNLTAA CRAFIMEPMW
     NPAAEAQAVD RIYRIGQKRP VLVKRYQMRD SIERKIVELQ KRKQQLADVS LNQNHKQLSK
     KEVREQHMKE ILALFK
//