ID A0A1V6SLU9_9EURO Unreviewed; 1479 AA.
AC A0A1V6SLU9;
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=PENFLA_c034G05000 {ECO:0000313|EMBL:OQE15027.1};
OS Penicillium flavigenum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=254877 {ECO:0000313|EMBL:OQE15027.1, ECO:0000313|Proteomes:UP000191342};
RN [1] {ECO:0000313|Proteomes:UP000191342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 14082 {ECO:0000313|Proteomes:UP000191342};
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:OQE15027.1}.
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DR EMBL; MLQL01000034; OQE15027.1; -; Genomic_DNA.
DR STRING; 254877.A0A1V6SLU9; -.
DR OrthoDB; 8175at2759; -.
DR Proteomes; UP000191342; 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; 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; PF13920; zf-C3HC4_3; 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:UP000191342};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 341..539
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1142..1180
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 745..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..768
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1479 AA; 167871 MW; 5D66BCAC125D7467 CRC64;
MSVVVEEITL PDATLEPLYS IFQQCDDRPA KRRKTTKRGA RSLIQENGVS TAGVPLGYIP
LARLTMRIKP SNTNTNKYQR PYNPDLSTSS VPILIDVRSV HFLDEDLDNA SQPDPAEDGA
DRMELELSSL DEKELLIYPC EDLRLFELLA QLQAASRLAH VDKFSKKVPT ACYQAHLCAL
PDGAGFSLET VVLWKDSIEV PDPNRLGVAD LEAFTKYVRQ EKYVRPSADP REYRESMLGT
PKEWSPRDFY KNVHVPKVTD SSNIKCPDLK CKLFPFQQRA VRWLLQREGR DVGPNGEIMP
IGEPPKSDIP ASFNSMKDAD GRTYYFSHLF MVLTTDLSLW YDAADNLKGG VLAEEMGLGK
TVEVIALISL NKREESKIWK ADADGLRPTG GTLIITPPAI LEQWKQELKE HAPTLSVHHY
NGIKRSGQAT DDMIVDELAE FDVVLTTYNV IAKEIHYTGG GPQRALRHEK RFAQRKTPLV
RLSWWRVCLD EAQMIESGVS NAAKVARLIP REMAWAVTGT PLRRNIDDLF GLLLFLHYEP
FCFSAPLWRR LCLCFGPVLA KIINTIALRH RKGQLLEELR LPPQKRIVIT TPFTAIEEQK
YGQLFEQMCE ECGLNASGAP LRGDWDPEDF VIVEKMRTWL TRLRETCLRP NIRYRRTLGQ
GSGPLQTVGQ VLEAMTDANE AAIRAEERSL LLSQLRRGQL LENAKRRQEA LALWQNALDH
ATRLVEDSRE QLRLLKTKGA TSDKDGTTLG LINQDGEDDE DEEDEEAGNN SRLGECRLKL
RAALEVQHIA VFFTANAYYQ IKSDPNLTQP DSDEFKALEK REEEAYEAAK VIRKEMLTDI
ARRVERYMRK VKIKARDKEF VHIPKMKPHL YSKGVEAYNL LSKFEDFCDA LNKNAEQYKE
WRDVMVRLVS QSLIDQEEEA KLEGDEYERS TKHQDEMYVY MEALRSMYSD RYDALTGYKN
TLISHEAKAG IIQAERGEGP SPQLFLKIMD TRSQLQPDPS LGSLRGIVSE LRKLVASLEW
QAGSGNSRAR AEHEIVEMVL KNAGQMIAEQ LKVSTKLSRE VESFRDIMNN RLEYYRHLQQ
ISDTVAPYDE ESAGKPLDES AFNLRLEQEE LIEGKIASLR SKARYLIHLR DDSSSDSNPR
ECIVCQSTFE VGVLTVCGHK YCKDCLRLWW TAHQNCPMCK RKLKRNDFHR ITYKPQELVV
QEEKTPVKLS YEGHSQNAIY SDISSGHLNE IKNIDLEESY GSKIDTLVRH ILWLREHDPG
AKSIIFSQYG SFLSSLQAVF GFLEISSTTI DSPDGIEKFK SDPAIECFLL HGKAQASGLN
LTVATHVFLC EPLINTAIEL QVIARVHRIG QHRPTTVWMY LVSGTVEESI YEISVTRRLA
HITEKEKQAK AALSTSPADD DGVTEAAIES ANSMELQDAT LTTLMQRGSE GGEMVKKDDL
WQCLFGNTKQ KDGTNPSAEA EWEVGRFLRG EAAEQRREG
//
