ID A0A1V6Q476_9EURO Unreviewed; 1491 AA.
AC A0A1V6Q476;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENANT_c014G04668 {ECO:0000313|EMBL:OQD84060.1};
OS Penicillium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD84060.1, ECO:0000313|Proteomes:UP000191672};
RN [1] {ECO:0000313|Proteomes:UP000191672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
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:OQD84060.1}.
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DR EMBL; MDYN01000014; OQD84060.1; -; Genomic_DNA.
DR STRING; 416450.A0A1V6Q476; -.
DR OrthoDB; 8175at2759; -.
DR Proteomes; UP000191672; 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; 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; PF00271; Helicase_C; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000191672};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 349..547
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1149..1187
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 1491 AA; 170220 MW; AE8E0D899C41C96F CRC64;
MSVVVEEITL PESRSESLHR IFEQSVAPNS DAHPAKRRKV TQSRPKCLVT EKGKSATGIP
LGYIPLARLT LRMKSSSSTI IKGEQLQRLE PFPSRIPVVT EVRNIRLLDD DENNAPQQKS
LDLEAYVMEL RINDLEGKHS FSHSFQDSRL FDLLEQLRHA SGLAHANKYS NDAPIACYQA
SISVSPDRDV FTLDAVVLWK DSLEIPVLSY LQDPALEVFT RYVLQEHIDH PSTVYDRDQR
RERMLGIPQK WSPREFYSSV HVPRTTEGAS NLTCPDIDCD LFPFQKRALR WLLEREGMAV
QQDGTVVPME QIPENELPVS FREMKDADGQ TYYFSRLFMT LTTDISEWYD ASNLLKGGIL
AEEMGLGKTV EMIALISLHR RLSEQQQKAG LDGLKPSGAT LIITPPAILE QWKQELSKHA
PNMRVHHYTG IKRGKEETDD MIVDELAQFD VVLTTYPVIS REIHYAGVAP ERNLRHTKRF
EPRKTPLVRI SWWRVCLDEA QMIESGVSNA AKVARLIPRE IAWAVTGTPL RRDIDDLFGL
LLFLHYEPFC FSNPLWKRLF SRFGPVLVTI INKIALRHSK DQVRDELRLP PQKRIVITTP
FTAIEEQRYG QLFEQMCEDC GLDASGAPVR GNWDPEDPVI IEKMRVWLTR LRKTCLHPEV
SSSTRRALGA NNGPLRTVDE VLEVMIEANE TAIRAEERSL LLSQLRRGQL LENAKRRVEA
LVLWQKALDH ATQLVEKSRE QLRQQRLKSD SATDGINGTI SAMEHLNGDE AEDADNNSRL
GQYRLRLRSA LEVQHIAVFF TANAFYQIKS DPNLTQPDSE EFKSLEKREE EGYEAAKTIR
KEMLTDISRK VERYMKTIKE KTRNKQFVTI PKLKPYLYSD GLESYRLLMR FENLCVALNR
HAEQYNEWRT AMIKLVSQSL IDQEEDAELE GNEYERSTKH QDEMYVYMEA LRSMYADRHD
ALTGQKNVLI SHEVKAGIVQ AQRGEGPSPQ LFLRVMDTRS ELMPDPQLGS LRGIVSELRT
ILTSLDWQAS AGSSRARAEH EMVDLVLRNA GQMISEQLKV SSNLEKEVEM FRDTMNNRLE
YYRHLQQISD TVAPYDEESA GKPLDDELFN SRLRQEEILD GKISSLKSKG RYLIHLRDDS
SAENTSRICI ICQSTFEVGV LTVCGHKYCS DCIRMWWRSH KSCPMCKKTL KLKDFHQITY
KPQELVAQEE ESSVKPGHEQ HAQNAIYSDI SSGLLKEIKN IDLDDSFGTK IDTLARHILW
LREHDPGAKS IVFSQYKSFL TVLHEAFYRF KIVSSSIDRP DGIESFKKDP AVECFLLHGK
AQSSGLTLIN ATHIFLCEPL INTAIELQAI ARVHRIGQHR PTTVWMYLVS GTVEESIYQL
SVTRRLAHII EKEKHGKIGH SAGAPNGNGP LIEDLTETAI DSANSMEMQE ASLTKLMTSG
PSDGELVKQD DLWQCLFGGT VDKDSNNPSM EAEREVGRFL RGEAAEQRRI E
//
