ID A0A0D7AB18_9AGAR Unreviewed; 1414 AA.
AC A0A0D7AB18;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=FISHEDRAFT_44377 {ECO:0000313|EMBL:KIY47840.1};
OS Fistulina hepatica ATCC 64428.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Fistulinaceae; Fistulina.
OX NCBI_TaxID=1128425 {ECO:0000313|EMBL:KIY47840.1, ECO:0000313|Proteomes:UP000054144};
RN [1] {ECO:0000313|EMBL:KIY47840.1, ECO:0000313|Proteomes:UP000054144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 64428 {ECO:0000313|EMBL:KIY47840.1,
RC ECO:0000313|Proteomes:UP000054144};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
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DR EMBL; KN881914; KIY47840.1; -; Genomic_DNA.
DR OrthoDB; 8175at2759; -.
DR Proteomes; UP000054144; 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; 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; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000054144};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 203..457
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1070..1110
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 677..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 623..650
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1414 AA; 159432 MW; 5ECC64079AA15F33 CRC64;
MSIPPVEANL DVRAHDLPES VDDLFQACIT LAEAERAAIE ARLVVVPVAH TEADVVCTLR
VQVQVYLLPT IFEPPARSLE DAQRRVLYHI FPLSQASARP STGGATDIPF FFSVVGPAPA
TDVASAMQPA DLLPTLLPFQ RRSVAWLLRR EGFVFPSNDR KAVLCRIPIS TFSFWSPVPV
GYMHSLTGAL VRNLADLNGE EDEATTADIS GAILAEEPGL GKTLETIAVI MLTRPFASTR
DPRGTPRWDP QTKLQVHVVK STLVVTPPAL ASQWVEELRT HAPTLRVLVY DGWQKVEIPL
NNSSAERDRV KRLKSRTSSL LKKRKLAKAL KANSDDEDVD VQPPAPTLED WSTYVHEYDV
VITTYRVLQQ DLFVARPPPS RPRRADVVYT SLDRARSPLV SVEWDRVVMD EVQMVGGGKA
ADMVSLIPRR ASLAVSGTPA KTQVSDLLHV LRFLRVEDVM GSTKLWTRLL KPAFAQHFAA
FMNEYTIRTM KSAIQDELTI PQQTRYLVGI EMGPIERHVY DEALERVLLD LGLDSRGVAS
VEGWEPDANL LRSSIRRLRA ICTHPQVGQL QHERMTRTVL KSMSEVLEGM RDQNWRDIMD
DFKLHVQAQI RLAQLHMLDE ANVKRYQKSL ELLEAAGKDV ENLCREVEDA LLVLNDNNDA
SITANKCAET ESVDAKGKGR GREVDDDRSD DEISSDYGGQ ESLAETHMRI KKQALQSRLR
ECRMVLHRVW FLKGDIFHML GNTDAENQAY ANAQQIRHNL LKATAADAMR AMAELAHHWV
SGQAPLIQTP YLPESSSRTD ELTREGNSII ENVLNAQSRL LWEWRAHIKE LLTLPLGSED
DQEADGMEFQ RSLDTQGEAE TYLQVYAALL ADRKQALINE RTLLAAHAIK EKKKRTTKTA
AEAVDEIPDE VREAIDLQLE HTILQQMLTV RRKALLEGLN QRALKSVRND LIAAGAKLDK
KSPEKKEIED IVKSLKELMM EQNRVGEKLD SDIALLRRAF NQRILYFRQL QQISDTVEEL
KYELTLENAL ADTRLELAEL DAKIKTNRAR QRYLQQIDRR DESDEDEDCC ILCRCEFKRG
FMTQCAHMFC EDCMKLWILK KAGKTCPVCR VGIDPDTMQR FTVEEKNPVE SSKPANTEPV
PKSRREIDYN FIDPRVLAEI RDIDTLGDYG QKIQTLIRHL LYLQITDAGA KSIVFSAWAD
SLTILQRALT ENGILCVRID RASKGKSAVQ RFKEQDEISV LLLHGERENA GLNITCASRV
FLLESVVHHG FEIQAIARID RMGQTRPTEV YCYYAQDTIE KNILDLAARR GLSLYTRENY
RGTVNVSSFA ADAQKTVESP RKNKVKGDFI FKVDDMLAVL FPHMYEEVQY LVEDAAMTID
EPAEISVNGV ITSGSKQGWQ AWPNAVAGPS SLLA
//
