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Database: UniProt
Entry: A0A0G2FYF0_9PEZI
LinkDB: A0A0G2FYF0_9PEZI
Original site: A0A0G2FYF0_9PEZI 
ID   A0A0G2FYF0_9PEZI        Unreviewed;       416 AA.
AC   A0A0G2FYF0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   22-FEB-2023, entry version 27.
DE   SubName: Full=Putative ribonucleoside-diphosphate reductase m2 subunit {ECO:0000313|EMBL:KKY38869.1};
GN   ORFNames=UCDDA912_g01130 {ECO:0000313|EMBL:KKY38869.1};
OS   Diaporthe ampelina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX   NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY38869.1, ECO:0000313|Proteomes:UP000034680};
RN   [1] {ECO:0000313|EMBL:KKY38869.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY38869.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY38869.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY38869.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAY-2015) 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:KKY38869.1}.
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DR   EMBL; LCUC01000045; KKY38869.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2FYF0; -.
DR   STRING; 1214573.A0A0G2FYF0; -.
DR   OrthoDB; 5487627at2759; -.
DR   Proteomes; UP000034680; 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   Reference proteome {ECO:0000313|Proteomes:UP000034680};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        236..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          386..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        395..410
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   416 AA;  47276 MW;  50BA989A62CAC874 CRC64;
     MSVEITPSKQ VASGIESLNM ESPVKKLDLG IANKENDFQD PAVATLAQDL DTKHAATKEI
     IKAPEEPAQI PDLRGDELEE PILKENPHRF VLFPIQYHEI WQMYKKHEAS FWTAEEIDLS
     KDMHDWSNRL TDDERYFVSH ILAFFAASDG IVNENLVERF SGEVQIPEAR CFYGFQIMME
     NIHSETYSLL IDTYIKEPAQ RTHLLNAIDT IPCIRKKADW ALKWIQDRES TYAQRLVAFA
     AVEGIFFSGA FASIFWLKKR GLMPGLTFSN ELISRDEGLH TDFACLLFSH LKNRPSKQRV
     QDIITEAVAI EKEFLTEALP CALLGMNSNL MKQYIEFVAD RLLVALGNDK VYKSSNPFDF
     MENISLGGKT NFFEKRVGDY QKAGVMASTK KPVSADETGP EEKGENGGDF TFDEDF
//
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