ID A0A0D1Y980_9EURO Unreviewed; 953 AA.
AC A0A0D1Y980;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIV77369.1};
GN ORFNames=PV11_09167 {ECO:0000313|EMBL:KIV77369.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV77369.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV77369.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV77369.1,
RC ECO:0000313|Proteomes:UP000053599};
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 sideris CBS121828.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR EMBL; KN846954; KIV77369.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1Y980; -.
DR STRING; 1016849.A0A0D1Y980; -.
DR HOGENOM; CLU_000315_2_5_1; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000053599; 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:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd16509; RING-HC_HLTF; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.30.70.2330; -; 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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014905; HIRAN.
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 InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45626:SF11; FAMILY HELICASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G06590)-RELATED; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF08797; HIRAN; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00910; HIRAN; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053599};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 376..552
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 708..746
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 780..949
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 227..254
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 31..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 953 AA; 106293 MW; 6DB0C569E568E4E0 CRC64;
MTQGKRKAVE TIDLTADDDL PAPPRAKVPK PASSFSSQKS RGHLPTPPSS SQPGYGGSQS
HNNYPSFSSS QTHSQQDRNA WLSTQEQEAD IAREIDLTED FDDDVYENYR LYGIYDTKIV
GCRFYDGQAT VGEYVKVRRE PSNPYDSNAI RIDNVLRDQI GHLPRQVAAK LAPLIDSGQL
LIEGALTGAK SYYECPIGLK MFGTSDPVAG AALAQKMKDL KLPVKEYNQS KKRVQELEKE
RKAREKAAAD MAKKGNAVID NEGPNRYSNI NTATMSSTQT QESLDQVLSG TTTFNPRDVQ
DVVNKIGATE DVLEKMPMAE QPGALATILL PYQRQGLQWM LDHESPQLPQ KKDDVVQLWK
KAGNFYTNIA TNFSFSKAPE LASGGILADD MGLGKTIQVI SLIMADAHKD GQPTLIVAPL
SVMSNWSQQA SLHVKEKFAP RVLTYHGQGN KDLTPEQFKD YDIVITTYQT MTQELFGFGG
DKAKKVPTNK GLFSLIWRRI VLDEGHQIRN PKAKMSQAAC TLMAQSRWVL TGTPIVNNLK
DLYSHVKFLR LSGGLTEFEI FNSTLIRPLK NGNDGARLLL QALMSTLCLR RMKDMKFIDL
KLPEITFHKY AVKFLPHEQE RYDAFKSEAK GLLEAAKAKK GDTNMTHLLE VLLRLRQTCN
HWKMCGDERI KRLLELVEGN TIVDVENAAN RKALQDLLQL AIDSQEDCPV CLDSLKNPVI
TACAHTFCRE CIERVIETQH KCPMCRAELL DKEKLVDPAA GIGEGDEPDL DIDPDNTSSK
IEALIKVLKA SEKDRNVKTV VFSQWTSFLN LVQAQLERNG LNFTRLDGKM NSTRRDAAID
SLNTDPSCRI MLASLSVCSV GLNLVAANQV ILADSWWAPA IEDQAVDRVH RLGQTRDCKV
VRLIVEGTIE DEVLEIQAKK RQLASEAFGE KDGGKKRKEQ RAGTLRDIER MLG
//
