ID A0A0M8MYN8_9BASI Unreviewed; 945 AA.
AC A0A0M8MYN8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Dna repair protein rad5 {ECO:0000313|EMBL:KOS16201.1};
GN ORFNames=Malapachy_3153 {ECO:0000313|EMBL:KOS16201.1};
OS Malassezia pachydermatis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=77020 {ECO:0000313|EMBL:KOS16201.1, ECO:0000313|Proteomes:UP000037751};
RN [1] {ECO:0000313|EMBL:KOS16201.1, ECO:0000313|Proteomes:UP000037751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 1879 {ECO:0000313|EMBL:KOS16201.1,
RC ECO:0000313|Proteomes:UP000037751};
RA Triana S., Ohm R., Gonzalez A., DeCock H., Restrepo S., Celis A.;
RT "Draft Genome Sequence of Malassezia furfur CBS1878 and Malassezia
RT pachydermatis CBS1879.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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:KOS16201.1}.
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DR EMBL; LGAV01000001; KOS16201.1; -; Genomic_DNA.
DR RefSeq; XP_017993833.1; XM_018137631.1.
DR AlphaFoldDB; A0A0M8MYN8; -.
DR STRING; 77020.A0A0M8MYN8; -.
DR GeneID; 28729507; -.
DR VEuPathDB; FungiDB:Malapachy_3153; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000037751; Unassembled WGS sequence.
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; 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 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 PANTHER; PTHR45626:SF22; DNA REPAIR PROTEIN RAD5; 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 SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00910; HIRAN; 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; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000037751};
KW Zinc {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 330..527
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 700..745
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 776..941
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 945 AA; 106738 MW; 3C2A4B4309BC344E CRC64;
MVSLEADDTS APLFFLEGDA GSTDLVAKKR PRSDHPAEES WRRRYLGTFV LCGYSMTKGS
DYIHAGDRVL IQRKAKATAK PKGTRGRGGK KQDRADYVVR FSNTRGFEVG RIPIDVAGWM
SCLLDAKLAE FDGIVVDCPS SLEVGSDILL EIKAYLCRST FESSLTRSCH LTTQMAEKPM
LESEESEQER HLRHRKVSLQ RLFRTCHLVP SKKATHTPHH KLTRVKRDDE DDGTEVSDTC
LHDIYAKAQQ DDASLPFAEP PSTFALTLRP YQKQALGWMQ TMEAAEGPSR EQTLHPLWEE
YQFPLADDED AGFGTFYMNP YIGDLSLDFQ PMSRGARGGI LADEMGLGKT IMLASLIHAN
RMADTTRSRP ARTRMQQTPL SFTKAAKRQG PSKATLVVAP MSLLSQWRTE LQRASAPGSL
NVVVYYGDVR DQLASQLAQS QADVVITSYG TLTSDYKQLE KKGPSPLFAE SWHRVILDEA
HTIKNRSTLA ARAAYQLDAD RRWALTGTPI QNRLTDLYSL LRFLRVEPWG DVSFFNSFLA
KPFASQNEKA LDIVQAILSS ILLRREKHSK DRDGRLIVEL PPKIIDTQHL TFSQAERDIY
NNVYERARTQ YRDLVRQGLV GKHFSLIFAV LMRLRQAVCH PYLVLQKGAN ESSAPEERSY
EDQLRELVRR FEAGDQSEDA YARDVLDTLL SSDTSEEEEC PFCMELKPSK CFLPLCMHHG
CRECLVQYLQ SCEDRGEVPH CPVCRRGPVQ VEDLVESVRP AKDVAPPTAP IRSSTKLDAL
MAQLATITHA EPDCKGVIFS QFTRFLDLIQ THMQQQGYSC VRLDGRTSQK ERKRVLSQFA
SEPAPLFLLI SLRAGGVGLN LTAANHVWLM DCWWNSSIED QAIDRIHRLG QTRTVTVHRL
LVEQTIEDRI LAIQRHKNEL VHHALASTPR DGTSDTMENL RLLFD
//
