ID A0A093V6E3_TALMA Unreviewed; 528 AA.
AC A0A093V6E3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 27.
DE SubName: Full=LON peptidase N-terminal domain and RING finger protein 1 {ECO:0000313|EMBL:KFX48137.1};
GN ORFNames=GQ26_0131980 {ECO:0000313|EMBL:KFX48137.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX48137.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|EMBL:KFX48137.1, ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|EMBL:KFX48137.1,
RC ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
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:KFX48137.1}.
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DR EMBL; JPOX01000013; KFX48137.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093V6E3; -.
DR HOGENOM; CLU_515983_0_0_1; -.
DR Proteomes; UP000029285; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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); 1.
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; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00464; LON; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
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 Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 180..218
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 263..490
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 528 AA; 59877 MW; E8787517B4C69974 CRC64;
MSMIPYNERD LYTYQSSNNI DEADESTGSS ETQENTPSTI DDNTLSSSVR KDDLSFLSSA
VEETRGNFVF AGEDFGVFEK VANDFEDGKQ QWSGTDVCMQ WKMTMHATGV ADEAETESDD
VTTHPKEEGR LPYDAGDVVY EDTAVINNEK EELLNDDTSN KIDEVIYEQL RTGIRDELDC
RVCYGLIVDP CISPCGHSFC YECANRIRDT SNLCPLCRKK MDLSFREGPN PAHGVLRCLL
DAFFPDEIKS RKEAIEEDGT CDDDELPLFV CTLAFPSTST HLHIFEPRYR LMIRRALDSG
NSKFGMVTHN FYHDLATEGH PDRSPEPFMQ YGTAVRIEWR DFLPDGRIML TAVGMHKFKI
LRYGVLDGYY RAHTERVDDI SLAEEETLEA RELAAANQNN QPANGSPLNA LSTQQLMQIC
MDFLEKQRMN SAPAVRERIN RVFGQPPTDP AIFPYWFANV LPIPDEEAYK IIPLTSVRER
LKVAATWPDN HHWSNSTPFD VAGDESNEAC IALEKARAVA RRRRGMLR
//
