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Database: UniProt
Entry: A0A0N0TQF3_9ACTN
LinkDB: A0A0N0TQF3_9ACTN
Original site: A0A0N0TQF3_9ACTN 
ID   A0A0N0TQF3_9ACTN        Unreviewed;       396 AA.
AC   A0A0N0TQF3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=MDMPI N domain containing protein {ECO:0000313|EMBL:KOX21143.1};
GN   ORFNames=ADL06_26340 {ECO:0000313|EMBL:KOX21143.1};
OS   Streptomyces sp. NRRL F-6491.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1519495 {ECO:0000313|EMBL:KOX21143.1, ECO:0000313|Proteomes:UP000037743};
RN   [1] {ECO:0000313|EMBL:KOX21143.1, ECO:0000313|Proteomes:UP000037743}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL F-6491 {ECO:0000313|EMBL:KOX21143.1,
RC   ECO:0000313|Proteomes:UP000037743};
RA   Noorani M.;
RL   Submitted (JUL-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:KOX21143.1}.
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DR   EMBL; LGEE01000243; KOX21143.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0TQF3; -.
DR   PATRIC; fig|1519495.3.peg.5602; -.
DR   Proteomes; UP000037743; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 1.10.10.1320; Anti-sigma factor, zinc-finger domain; 1.
DR   Gene3D; 1.20.120.450; dinb family like domain; 1.
DR   InterPro; IPR041916; Anti_sigma_zinc_sf.
DR   InterPro; IPR034660; DinB/YfiT-like.
DR   InterPro; IPR024344; MDMPI_metal-binding.
DR   InterPro; IPR027383; Znf_put.
DR   Pfam; PF11716; MDMPI_N; 1.
DR   Pfam; PF13490; zf-HC2; 1.
DR   SUPFAM; SSF109854; DinB/YfiT-like putative metalloenzymes; 1.
PE   4: Predicted;
FT   DOMAIN          39..68
FT                   /note="Putative zinc-finger"
FT                   /evidence="ECO:0000259|Pfam:PF13490"
FT   DOMAIN          119..265
FT                   /note="Mycothiol-dependent maleylpyruvate isomerase metal-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF11716"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   396 AA;  42473 MW;  D19B41DCCF369C1A CRC64;
     MAGRPEEPDL TGRPEEPEAR EPEGEEPDVP VLTHGVLKSL LGAWALSACS AGETAAVEAH
     LTECGPCADE ALRLRDAVAL LHRDRDLDLD PLLRSRVLEN CLGRRPARIP VPDWVTPYDA
     ETARLDALLR DIGESEWHAP VRLKWYEKDR PVRRKATVAG VIGHLFAVDG LVAGALGLDD
     PLGAGTPELS PSERTEAFWS ALERPPGRAL REPWRDQSHT LIRTVSFAGR GVADLTVTYK
     DFALPLRDSL LERAFECWLH ADDIANAVAY PYEPPCGAHL HGMIDLATRL LPAALAGRRR
     AGLASPARGL VAAGAPGRSL HLEVEGAGGG HWYIALDSPA AVGDPDRAVA QVAMEGVEFC
     RLVAGRVSPE EAAAGQDGDR EAIRDVLGAA ASLSRL
//
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