ID   A0A366QRD1_9HYPO        Unreviewed;       409 AA.
AC   A0A366QRD1;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RBR07469.1};
GN   ORFNames=FIESC28_10627 {ECO:0000313|EMBL:RBR07469.1};
OS   Fusarium coffeatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium incarnatum-equiseti species complex.
OX   NCBI_TaxID=231269 {ECO:0000313|EMBL:RBR07469.1, ECO:0000313|Proteomes:UP000253153};
RN   [1] {ECO:0000313|EMBL:RBR07469.1, ECO:0000313|Proteomes:UP000253153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FIESC_28 {ECO:0000313|EMBL:RBR07469.1,
RC   ECO:0000313|Proteomes:UP000253153};
RA   Gardiner D.M.;
RT   "Fusarium incarnatum-equiseti species complex species 28.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC       chain family. {ECO:0000256|ARBA:ARBA00009303}.
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:RBR07469.1}.
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DR   EMBL; QKXC01000315; RBR07469.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A366QRD1; -.
DR   OrthoDB; 5487627at2759; -.
DR   Proteomes; UP000253153; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:InterPro.
DR   CDD; cd01049; RNRR2; 1.
DR   Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 1.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR012348; RNR-like.
DR   InterPro; IPR033909; RNR_small.
DR   InterPro; IPR030475; RNR_small_AS.
DR   InterPro; IPR000358; RNR_small_fam.
DR   PANTHER; PTHR23409; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN; 1.
DR   PANTHER; PTHR23409:SF18; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M2; 1.
DR   Pfam; PF00268; Ribonuc_red_sm; 1.
DR   SUPFAM; SSF47240; Ferritin-like; 1.
DR   PROSITE; PS00368; RIBORED_SMALL; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        232..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          29..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          384..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        384..403
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   409 AA;  46381 MW;  E4923D2E98FB773F CRC64;
     MASQMTPSKQ AASAIENFNM ESPVKKLDFG AANKENEPLS NTKETNELKT KAVEEIKKDD
     SKVSVAPGIK AEEADEPLLQ ENPQRFVLFP IKYHEIWQMY KKAEASFWTA EEIDLSKDLH
     DWNNRLTADE QFFISHILAF FAASDGIVNE NLVERFSGEV QIPEARCFYG FQIMMENIHS
     ETYSLLIDTY IKEPAQRTYL FNAVDTIPCI RKKADWAIRW IQDKNSSFAQ RLVAFAAVEG
     IFFSGAFASI FWLKKRGLMP GLTFSNELIS RDEGLHTDFA CLLHSHLKGR ASKQMIQDII
     TDAVTIEQEF LTEALPCALL GMNSNLMKQY IEFVADRLLV ALGNEKVYKA TNPFDFMENI
     SLGGKTNFFE KRVADYQKAG VLHSASKKAD EEESPKGENG GDFTFDDDF
//