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Database: UniProt
Entry: A0A1E1KMV5_9HELO
LinkDB: A0A1E1KMV5_9HELO
Original site: A0A1E1KMV5_9HELO 
ID   A0A1E1KMV5_9HELO        Unreviewed;       416 AA.
AC   A0A1E1KMV5;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   28-JUN-2023, entry version 26.
DE   SubName: Full=Small subunit of ribonucleotide reductase {ECO:0000313|EMBL:CZS99368.1};
GN   ORFNames=RCO7_00607 {ECO:0000313|EMBL:CZS99368.1};
OS   Rhynchosporium commune.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Ploettnerulaceae; Rhynchosporium.
OX   NCBI_TaxID=914237 {ECO:0000313|EMBL:CZS99368.1, ECO:0000313|Proteomes:UP000178129};
RN   [1] {ECO:0000313|EMBL:CZS99368.1, ECO:0000313|Proteomes:UP000178129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UK7 {ECO:0000313|EMBL:CZS99368.1,
RC   ECO:0000313|Proteomes:UP000178129};
RA   Ploux O.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC       chain family. {ECO:0000256|ARBA:ARBA00009303}.
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DR   EMBL; FJUW01000016; CZS99368.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E1KMV5; -.
DR   STRING; 914237.A0A1E1KMV5; -.
DR   InParanoid; A0A1E1KMV5; -.
DR   OrthoDB; 5487627at2759; -.
DR   Proteomes; UP000178129; 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:UP000178129};
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          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          389..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   416 AA;  47220 MW;  7A7DE2EE48DC24FF CRC64;
     MTSQVTPSKT AATGIESLKM GDSPMKKLNF GTANKENEPL SVDAPASEDI EVKKPIVEEI
     KKAEISAMVA KGFKPEEADE PLLRENAQRF VLFPIKYHEI WQMYKKAEAS FWTAEEIDLS
     KDLHDWNNRL NDDERYFVSH VLAFFAASDG IVNENLLERF SGEVQVPEAR CFYGFQIMME
     NIHSETYSLL IDTYIKEQAQ RTYLFNAIET IPCIKKKADW AVRWIQDKDS TFAQRLVAFA
     AVEGIFFSGS FASIFWLKKR GLMPGLTFSN ELISRDEGLH TDFACLLFSH LNHRPSKQAV
     QDVITEAVEI EQEFLTDALP CALLGMNAAL MKQYIEFVAD RLLLALGNEK YYKSANPFDF
     MENISLAGKT NFFEKRVADY QKAGVMAGTQ KKHEDTAAQT EAKAENGGDF NFDEDF
//
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