ID A0A0W0FU71_9AGAR Unreviewed; 1676 AA.
AC A0A0W0FU71;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KTB39736.1};
GN ORFNames=WG66_7691 {ECO:0000313|EMBL:KTB39736.1};
OS Moniliophthora roreri.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB39736.1, ECO:0000313|Proteomes:UP000054988};
RN [1] {ECO:0000313|EMBL:KTB39736.1, ECO:0000313|Proteomes:UP000054988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB39736.1,
RC ECO:0000313|Proteomes:UP000054988};
RA Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT pod rot of cacao.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:KTB39736.1}.
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DR EMBL; LATX01001642; KTB39736.1; -; Genomic_DNA.
DR eggNOG; KOG0298; Eukaryota.
DR Proteomes; UP000054988; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
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; IPR018957; Znf_C3HC4_RING-type.
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; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF00097; zf-C3HC4; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000054988};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 413..678
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1326..1366
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 42..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1648..1676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..940
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1648..1666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1676 AA; 189094 MW; B3F7861265D647E8 CRC64;
MRETISHHHE SLRTVHRDFG KPFRAILNLR NVAKLLQMNH CDNPEVDASK DDAENTGKGK
KRARTPSIQQ NAPNKRIKTL SGIPHRKDAS AEQNNPYPIK PMPYTKFANP YERSETRFSQ
DSQLIHVLSH TCEVHYTTED DGIEDTEWAA EEEWFRKELD KSFGAVTEPQ TVEFGALDFT
SLAGHMVVRS KLLTESGKDE SDWISLLPPV NPDAINASEH DIYPPELVDL FHSCDVLRIN
NRAHVNGRLR FIMLPPGVQE AGEERFRVQI EFSVSLVVPG IFKAAQRRNI EDAQRRLFSF
LHPSSPPPSS FTGANNISYY YSVMGPAPKL SHMAEEAMQS DALHSTLLPF QRRTVGWLLE
REGMSVSEDG TIRPKSSDSS PEFSFWERVP VTEGEEWWYN RLTGALSDTR PETKTTLSSF
GGILAEEPGL GKTVETIALV CLNPAPADRT PALSRWEPEA KVEVKAVKAT LIVTPQALQS
QWIDEIKAHA PHLKVLVYDG WSKLDVPLTA SQIEEAKQKR ALKKKKAKKK AERANTVAEA
VARMRGKGKG KVKADENQGE EQEEDDDDVV DWYTYAHGFD IVITTYTVLQ SDLNVARAPP
TRPRRTGVSY ANIERQRSPL VCCEWYRVIM DEVQMAGGGK VEDMVSLIPR RTSFAVSGTP
ARTQVADLVH VLKFLRVYQT QVSSTRLWSR LLLPGFARQF ADLFGHYSVR TMKSAVKDEL
TIPQQTRYLV SIDMGRVERH VYDQTLETVL LELGLDARGV AASEGWEIDG TLLRASIRRL
RAICTHPQVG QLAKQNGAEK LNKPGVLKTM ADVLQMMKDQ NWRTLIEDCK AKVQTLIKIA
QLQMLDASVL NRYQLVLETL STAEKEANKL MEDVEAALTD HRTKGEVLRK EAAAQRELRA
QAQSHQQQSS GKGKERESSP LSEEEDDDDE DDDEDDDYKG IPETPEGKDY KDKLRALKSR
LREARFVLHR VKLLQGDTHH NLGPTHADQE NEAYEAAEQI RKTLLKTTES KAKKGMEQLT
LEATSTGVNA EELLIPVPFL EQGGIRSAEL IEEFHEIVEN VLNEQTTLLW QWRTEIYNLL
TQKLSSGADD EGDGADGHEY ERNLENQGKA EVYMQAYAAL LADRREALMN ERTLLAAHNV
KETKQRKTRA AMNAAGLADD AVVIPDDIEM KPEDEVLHKQ LSDTRKELLA LLEGRAVKSI
MVELSGALTR ITRDDDPERP LLKQTVTDLR RLIQQQQQML DKLDVDLGAF RKAFNQRVLY
FRQLQEISDS VAEVEYEGSR ALALEEAKKE KEDLDAKINR SRAHQRYLGN LADSHDEGDD
EDENCCILCR YEFERGFITM CAHAFCEQCM KAWLQRRDGK TCPVCRVLID TDKLQRFTLN
DPAKPPPPVV NGELAPKSTR RIEYNMIDPA IFKEIQKIDA FGDFGNKIQS LVRHLLYLQQ
NEPGTKSIVF SAWADSLTIV QQALTENGIR SIRIDRGARG EGPVIKFKND PDILVMLLHG
ERENAGLNIT CASRVFLLES VVHHGFEVQA IARIDRMGQT RPTEVYCYYA EETVERNILD
LAARQGLSLY TKENARGSLN TANFATSAEK QEIDSPAKRN AAKTQKGDFI SKIDDMLAVL
LPHMYEDVQY LIPEEDVVME DLTNVSSENL QARRSGNGSK GQQHVNAVAG PSRLKL
//
