ID A0A0P7BGP9_9HYPO Unreviewed; 568 AA.
AC A0A0P7BGP9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=LON peptidase N-terminal domain and RING finger protein 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=AK830_g539 {ECO:0000313|EMBL:KPM46002.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM46002.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM46002.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM46002.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:KPM46002.1}.
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DR EMBL; LKCW01000003; KPM46002.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7BGP9; -.
DR STRING; 78410.A0A0P7BGP9; -.
DR OrthoDB; 3088759at2759; -.
DR Proteomes; UP000050424; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16514; RING-HC_LONFs_rpt2; 1.
DR Gene3D; 1.20.58.1480; -; 1.
DR Gene3D; 2.30.130.40; LON domain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR003111; Lon_prtase_N.
DR InterPro; IPR046336; Lon_prtase_N_sf.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23327:SF42; LON PEPTIDASE N-TERMINAL DOMAIN AND RING FINGER PROTEIN C14F5.10C; 1.
DR PANTHER; PTHR23327; RING FINGER PROTEIN 127; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00464; LON; 1.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000050424};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 235..273
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 322..562
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 568 AA; 63627 MW; 1CF15D04D0FD4C60 CRC64;
MSPDAQPRAP ATSPPPAPRE SPGQDTDSNP DSDSDSDQDI APPTPTTPIQ PRDLVRLFQC
QICSLPLREP VSLPCGKSMC RRCLPKTHLR ANISYPGSPT RLQGFRCPFP TCHKEHALED
CAVDVILNKA TQQLKGDVDL VRNTAQVSGI STRIYTQNPW AIAGIGSMRD DDGSSQVFKG
GKLVATYTLA EDGDLQYQAE VLYDQASTTS SAEDDMNDDG LRRKTQVATR AEMDCQVCYA
LFYDPITTAC GHTFCRACLH RVFDHSRYCP VCRRELAINP LLNSTACPSN ETLGRIIQSF
WPDEVRIRRA TVAAESASQL EGYDFPLFIC TLAFPSMPTF LHVFEPRYRL LVRRVLEGDR
TFGMVLPKQS RGIGDPDFHE LGTLLRIVNV QYYPDGRSLI ETVGLSRFRI LRHGYLDGYT
VVKTERVADV SLQEEEAMEA AEAISQPAPQ DILTNDIKPA EEPLNPHSID RPGPITAADI
DKMSTQNLMQ FTSSFIARMR NRSVPWLTER MLAIYGECPD DAANLPWWFA SMLPVKDNEK
YRLLGTSSVR ERLKICCAWI LEWEAARW
//
