ID A0A1V6RII2_9EURO Unreviewed; 1452 AA.
AC A0A1V6RII2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENVUL_c042G02924 {ECO:0000313|EMBL:OQE01615.1};
OS Penicillium vulpinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=29845 {ECO:0000313|EMBL:OQE01615.1, ECO:0000313|Proteomes:UP000191518};
RN [1] {ECO:0000313|Proteomes:UP000191518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29486 {ECO:0000313|Proteomes:UP000191518};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:OQE01615.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MDYP01000042; OQE01615.1; -; Genomic_DNA.
DR STRING; 29845.A0A1V6RII2; -.
DR OrthoDB; 8175at2759; -.
DR Proteomes; UP000191518; 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; cd18070; DEXQc_SHPRH; 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; PF13639; zf-RING_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; 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:UP000191518};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 320..516
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1115..1153
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 28..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1452 AA; 164554 MW; F03FF4B211276FE8 CRC64;
MSVVVEDIAL PGTLLMQLLS LYTPSSNAMT VPPSGARQPK GAQGKPSDTS TRKYKRPYDL
GISISRVPVL IDVRSVHFID DDLNNTSQPD SANGDANRME LELSSLDEEG LLMYPCENLQ
LFDLLGQLQT VGKLAHVDQF SNNVPTACYQ AHLCVSPDGS GFTLEVVALW RDSLEVPDLN
RLTEADLETF TRYVLQEKCV RPSELTDPRE YRNKMLGIPK EWSPRDFYSN VHVPNATENS
TNLKCADLKC QLYPFQRRAV RWLLQREGRD VGPGGEIMPI GELPKSDLPA SFSSTKDADG
GTYYFSHLFM VLTTDISGWH DAADNLKGGI LAEEMGLGKT VEVIALISLN KREQQLKADL
DGLKHTRATL IITPPAIFEQ WRQELKEHAP TLRVHHYTGI KRGKETTDDM IVNELAEFDV
VLTTYNVIAK EIHYAATPPK RSLRHEKRFV QRKTPLVRLS WWRVCLDEAQ MIESGVSNAA
KVARLIPREI AWAVTGTPLR RNIDDLFGLL VFLHYEPFNF SAPLWRRLCV CFGPVLAKII
NTIALRHRKG QLLDELRLPP QKRIVITTPF TAVEEQQYGQ LFEKMCEECG LNASGAPLRG
DWDPEDPVII EKMRNWLTRL RQTCLHPQVG HRRVMGPGSG PLRTVDQVLE AMTESNEAAI
RTEERSLLLS QLRRGQLLEN AKRRQEALAL WQKALDHATK LVEDSREQMR LLTSKSTTSD
NNGATPGLIN PDNKDDEDEE AGNYSLIQCR QKLRAALEVQ HIAMFFTANA YYQIKSDPNL
TQPDSDEFKA LEKREDDAYE AAKVIRKEML ADISRKVERY MNEIKIKAQG RLFVNIPKMK
PHLYSKGVES YNLLTKFEDF CDALNKHANQ YKEWRDVMAR LVSQSLIDQE EETKLEGDEY
ERSTKHQDEM YVYMEALRSM YSDRHDALTG QKNNLISHEA KSGIAQAQRG EGPSPQLFLK
IMETRSQLMP DPNLGSLRDI VSELRKLVAS LEWQATLGNS RARAEHEVVE MVLKNAGQMI
AEQLKVSHKL SREVEMFRDT MNNRLEYYRH LQQISDTVAP YDEENAGKPL DEAAFTSRLE
QEESLESRIA TLKSKARYLI HLKDDDGSDN NVRECIICQS TFEVGVLTVC GHKFCKDCLR
LWWAAHQNCP LCKKKLKRND FHQITYKPQG LVVQEEKSHV KLDHEGHSQN AIYSDISSSH
LNEIKNIDLD GSYGTKIDTL ARHILWLREH DPGAKSIIFS QYGSFLSVLQ SAFRSLGIVT
TSIDASNGIQ NFKTDPAIEC FCLHGKAQSS GLNLTVATHV FLCEPLINTA IELQIIARVH
RIGQYRPTTV WMYLVSGTVE ESIYEISVTR RLAHIMEKEK QYKKALLDPP TDGDGVTEAA
IESANSMELQ DATLTTLMQR GDIGGEMVKK DDLWQCLFGN AKKKDGIDLS SEAEREVGRF
LRGEAAEQRM EG
//
