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Database: UniProt
Entry: A0A150UXT0_9PEZI
LinkDB: A0A150UXT0_9PEZI
Original site: A0A150UXT0_9PEZI 
ID   A0A150UXT0_9PEZI        Unreviewed;       769 AA.
AC   A0A150UXT0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=LIM zinc-binding domain-containing protein {ECO:0000259|PROSITE:PS50023};
GN   ORFNames=M433DRAFT_72874 {ECO:0000313|EMBL:KYG42883.1};
OS   Acidomyces richmondensis BFW.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX   NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG42883.1, ECO:0000313|Proteomes:UP000075602};
RN   [1] {ECO:0000313|EMBL:KYG42883.1, ECO:0000313|Proteomes:UP000075602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFW {ECO:0000313|EMBL:KYG42883.1,
RC   ECO:0000313|Proteomes:UP000075602};
RX   PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA   Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA   Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA   Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT   "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT   Carbon Cycling in Acid Mine Drainage.";
RL   Front. Microbiol. 7:238-238(2016).
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:KYG42883.1}.
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DR   EMBL; JPDO01000387; KYG42883.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150UXT0; -.
DR   STRING; 766039.A0A150UXT0; -.
DR   Proteomes; UP000075602; Unassembled WGS sequence.
DR   GO; GO:0030695; F:GTPase regulator activity; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd08368; LIM; 1.
DR   CDD; cd09397; LIM1_UF1; 1.
DR   Gene3D; 2.10.110.10; Cysteine Rich Protein; 2.
DR   InterPro; IPR001781; Znf_LIM.
DR   PANTHER; PTHR24207:SF1; FILAMIN-BINDING LIM PROTEIN 1; 1.
DR   PANTHER; PTHR24207; ZYX102 PROTEIN; 1.
DR   Pfam; PF00412; LIM; 2.
DR   SMART; SM00132; LIM; 2.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 2.
PE   4: Predicted;
KW   LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW   ProRule:PRU00125};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00125}; Reference proteome {ECO:0000313|Proteomes:UP000075602};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   DOMAIN          611..674
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          675..740
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   REGION          37..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          745..769
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..97
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..155
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..171
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..221
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..302
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..352
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..373
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..403
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..488
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        498..512
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        522..537
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        538..563
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   769 AA;  82945 MW;  113AE753BE97BD07 CRC64;
     MSLAASLSSD GMRPASFLPS IKCSSCGDEI EIAAMGDHTC NKAPPSPKAQ PASLSNPFTL
     RQLNANGVHT PSPLVQSHSA TSPQQQTPRT RVRAPTLTAN SMPAPKPMRP APPRINPEVA
     NLPFLAPRPP RSQSPMSPAV SVRSASSNGG SRPPPLRSMT SPAPRIFDPR PPSPELSSNL
     DCAFPPFPPP SSVGSSSRPG TSNGRNTPNS DRGSSRAGSR QGNRLAPDKD PFSATPRSPL
     GYSGDGLVQR NVDNDPPPLP TEPIPRPSTS HSVRSQIPSP LADSSTIGKF SPVDSQSTIE
     SKRGPPPRPE RPTEELLSPT FLDKLSAEPV AEMPSTFLPS QPSIPIRSTD RSKTFPLRQE
     SSDGPSPSHA LHKTPSEPQM RGRRPLASQT SNSEPSHIPQ LRPRSSSRGA LRMDLRLQDA
     PPVPLPVQHS EKTHQAGRHT PSESRSSTMS SGHSIHNSNS SVGPSPVGSA ASSVDAFSPL
     SYNSNNYAED ERMKVPGLNV KSSQQQKPGM RAEQPAQRSP PRNFARPSPP KQPPTNNYGL
     PKSPVSSAST RPRSKSNAAP SGAQYTPYKP YKPSPSVRSA SPQAAPALPP VPREPTRVQT
     PPSRRNTSAR PACRGCGKII EGKSVKAADG RLTGRWHKAC FTCRTCKQPF TTADFYVLDN
     QPYCEQHYHE KNGSLCHGCH RGIEGQYLET STSSRGGYMD KKFHPRCFTC FECRQVLSDD
     YFEITGKVFC ERHALAAMRS QAKMAGTGLH PPDRKALTTE RRTTKLMMM
//
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