ID D8QC03_SCHCM Unreviewed; 939 AA.
AC D8QC03;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFI94844.1};
GN ORFNames=SCHCODRAFT_58967 {ECO:0000313|EMBL:EFI94844.1};
OS Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX NCBI_TaxID=578458 {ECO:0000313|Proteomes:UP000007431};
RN [1] {ECO:0000313|EMBL:EFI94844.1, ECO:0000313|Proteomes:UP000007431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431};
RX PubMed=20622885; DOI=10.1038/nbt.1643;
RA Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA Woesten H.A.B.;
RT "Genome sequence of the model mushroom Schizophyllum commune.";
RL Nat. Biotechnol. 28:957-963(2010).
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; GL377309; EFI94844.1; -; Genomic_DNA.
DR RefSeq; XP_003029747.1; XM_003029701.1.
DR AlphaFoldDB; D8QC03; -.
DR STRING; 578458.D8QC03; -.
DR VEuPathDB; FungiDB:SCHCODRAFT_02585708; -.
DR eggNOG; KOG1001; Eukaryota.
DR HOGENOM; CLU_000315_2_5_1; -.
DR InParanoid; D8QC03; -.
DR OMA; ETTVWRL; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000007431; 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; 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; 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; PTHR45626:SF17; HELICASE-LIKE TRANSCRIPTION FACTOR; 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; PF00097; zf-C3HC4; 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 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:UP000007431};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 367..535
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 718..756
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 795..939
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 57..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 939 AA; 102458 MW; F21CCE809CE8937E CRC64;
MALLPELTYA PPRGCVTPVI LAQLSNVNLE TIEGFKDLQA HDRHKIREAV RLRRIDPADV
PPSARVAAAP PPASQTTRKR KAPEPTPQSS TSQASFSTPG PSRLSQAIED EATEDNTEEA
ADELYCTLST GVVGIQYYTG LVGAGEEVQL IREPNNRYDR NAIRVSNIAG SQVGHIPKNV
AARLAPLLDR GEITVEGVMK QGNCTCPRVV SEIRIYGRSD RRRELEPKLI WATPGQRGFE
QLRNPTASSY GGGGGGYGGG MPLPPIPTYT GAASGLEKVD DESRRNSVLD TLCSVDDVLK
LPEHPDPPGV AKGDLVVELL KHQKQALQWA IEHEYPKLPA SEKDPPVQFW QYKQMAGRVM
ATKTPQSTAP TLGKGALCAD AMGLGKTLTM IALILATKAD KPSGCIKGTL IVAPLSIISN
WEKQLEDHCA PGALKSCTYY GATRGMSAEE LKKYDVVITT YQVISGEWAD RAGTGQPARK
KKKGVAGGSL FDVKWKRIVL DEGHSIRNPR AKMTQACCAL EADRRWVLTG TPIPNLSLTA
PSQDLGSLLS FLRICKPLDE EDFFKRLLLR PLKAGDPSGA EILRVSRSMS ASFLQSLTRD
SEGTSLVPLP PVDVTVVPVA LDPETRASSL MSTVDILADV HAENIRRGRG INTASVLSML
TRMRQLALHP ALIPPDYLEQ LKAGQEQGGA APVKVISPAD RARLQAILAR HIEDCEECPI
CFTIPNDPRI TSCAHMFCLP CITEVIARDP KCPMDRRPLT LGDLIEPAPP MDLTQAPVSE
FEEDRTGIRA GSSAKIDQLV KLLQLNPPAD KSLVFSQFTS FLDKVSCQRW MRCIPYVRFD
GQMSGKRREE AIRRFSVPIK PTDTAASNWL PGGVNPKVML ISLKAGALGL NLTVANNVYL
WWQEGIESQA IDRVNRIGQT KPVHVYQMIA EDTVESKVR
//
