ID A0A1W2TLH6_ROSNE Unreviewed; 1428 AA.
AC A0A1W2TLH6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative rad8 protein and Rdh54p {ECO:0000313|EMBL:GAP89165.1};
GN ORFNames=SAMD00023353_0901770 {ECO:0000313|EMBL:GAP89165.1};
OS Rosellinia necatrix (White root-rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Rosellinia.
OX NCBI_TaxID=77044 {ECO:0000313|EMBL:GAP89165.1};
RN [1] {ECO:0000313|EMBL:GAP89165.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W97 {ECO:0000313|EMBL:GAP89165.1};
RA Kanematsu S.;
RT "Draft genome sequence of Rosellinia necatrix.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; DF977454; GAP89165.1; -; Genomic_DNA.
DR STRING; 77044.A0A1W2TLH6; -.
DR OMA; QLFEQMC; -.
DR OrthoDB; 8175at2759; -.
DR Proteomes; UP000054516; 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 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16449; RING-HC; 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; 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; PTHR45865:SF1; E3 UBIQUITIN-PROTEIN LIGASE SHPRH; 1.
DR PANTHER; PTHR45865; E3 UBIQUITIN-PROTEIN LIGASE SHPRH FAMILY MEMBER; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00487; DEXDc; 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 4: Predicted;
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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054516};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 322..534
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1125..1164
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1229..1387
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1428 AA; 160861 MW; ED6BA7D31E1581EC CRC64;
MSAIPRRAFG SKKKLGEEIK AYAHESFPNA LLGALRALAG HTLIDTDGSN EPPRKRPRVD
PMELDSIPVL QERFTISRPI GSCSPMAGQM AYNDAGHYLS FQLSREGLHI RSKAGAPCGP
FRCVLHLDQS FPDTTLAALT VLHQSREDNT QEGALTVSTT VSLRQDNTML HMHFTLDVNY
NTSTYASRNT KKRGLSQHIL NVLGEYKPDP SLPDHTMTAN EFYQAAFVPR SDNFNDLSSI
SIPGLEATLY PFQRRAVQWL LMREHVKYSR IGQGGELQLV AHPQPPEPIL PLSFSTANDV
NGRRFYVSHL YHVVTRDVTP FQESETSLRG GILAEEMGLG KTVEIISLIL AHKRGLCPLP
EIETCTSKVI HITGATLIVT PDTLQSQWLS EFKKHAPGLL VIKYPGMKVW ANDKAFGTKQ
TEGSLLDRLI STLVNCDVVI TTYSVLQAEL HYAMTPPERT MRYDKKHERH TSPLVQISWW
RVCLDEAQQI DSGVSSAAKV ACLIPRVNSW AVTGTPVKEG PNDLWGLLLF LHYEPFASCQ
FVWKALLKTH KFLFGPLFNR ITIRHAKQAV QDELRLPSQK RYVITMPFTN IEAHHYHSHF
RALIAKAGLN EQGIPFHADW KPDDSSVIDS LKMALASLRQ TILHPELGSG IAKVAAYRTL
AEHLDVMIEQ SEASIRTHQR LYLISKLNRA QLLENSPRVK EALKVWEEVL GEVKPTIVEL
REELGRTLQT ARQEQTKAAG SLIGEVYTDE ETLETAKVGE SRRKLRMFLE LHHRVAFLIA
SALFQIKSDE KFTQPDSDEF KHLEAREIEG YELARKIRRE ILQEPLTKVA KMIEKIQARA
STQSFVEIPE IITADMHGIE SVQITEALEN LSFSLNKQAN IIDEWREYVI QLLLTPPVDA
EGDEEVTGEE YEESAKVQDH LMVYTLALGA IIGDRQEALT GLVNERIRHE TTNAERMAKQ
GQGHAPDKML ELLRVRRDAK PFPDGSSLRG VVTASRELST KLRHDASAGS ARAATELQIV
NTQLRETQVI LTKQSKAVAS LERDLDFFTS AMNARVDFYR QLQSISENVA PIDPEAIGVG
DNLNRFWDNA LNDEAELKKK AEHWESNRRH LLYIKEEGSG SNDPCPICCS DDFIRGAITS
CGHTFCKDCI VHWLKSKSRC PICKEYQTPT MLSEFNKNEA VRKGLSLDTR LQGGPKREWG
VYTDIPNDIK HAIQNVKLHG PSYSTKVDTL MKHLLWLRDE EPGAKSIIFT QFRSFLRILE
QALAGHYIGF ATFTSLKHKS AQIQRFKDDP SVHCLLMDAK AHSSGLNLVN ANHVFLCEPL
LNTALELQAT ARVDRIGQEH ETTVWLYLVE GTVEGNIHDL SERRRLAYMG GDTQKGKSKR
PTEEEVMAAS LREFQESDLT KLMTESDEGE VVNKGDLWEC IFGRAMQV
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