ID A0A2H4UX67_9VIRU Unreviewed; 884 AA.
AC A0A2H4UX67;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=RR1 {ECO:0000313|EMBL:ATZ81504.1};
GN ORFNames=DiNV_CH01M_ORF22 {ECO:0000313|EMBL:ATZ81504.1};
OS Drosophila innubila nudivirus.
OC Viruses; Naldaviricetes; Lefavirales; Nudiviridae; Alphanudivirus;
OC Alphanudivirus droinnubilae.
OX NCBI_TaxID=2057187 {ECO:0000313|EMBL:ATZ81504.1};
RN [1] {ECO:0000313|EMBL:ATZ81504.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DiNV_CH01M {ECO:0000313|EMBL:ATZ81504.1};
RX PubMed=29155284; DOI=10.1016/j.meegid.2017.11.013;
RA Hill T., Unckless R.L.;
RT "The dynamic evolution of Drosophila innubila Nudivirus.";
RL Infect. Genet. Evol. 57:151-157(2018).
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406}.
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DR EMBL; MF966379; ATZ81504.1; -; Genomic_DNA.
DR OrthoDB; 2980at10239; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000290195; Genome.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000290195}.
FT DOMAIN 320..806
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 63..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..884
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 884 AA; 102250 MW; A77DBAFA3ACD35C2 CRC64;
MDRKNIETNA LGALINELST IHTYRYICNN SNYADVFEIT HADEEQSNEK NTCNNDVEIY
NNYDTTVDND DNNNKNGNDN DNQKNDINDN VNSKLNDTNN NIILNTNYDD VDIGLCTYYN
VNEPSMKTPY QLKLKFAQIY NSCGDKNCNI VDIAYNLDFI QEIDVYDGKS MEKRQLLEHT
IQMLYSDVVD IYEYRKVCDE IDPDSFKKWF PNYPLELLHW LDDDRDFIYN SHGLRLLKNR
YLRKNEPIQY CMLRIARLFV NCNDITNIST SEYHYWILYY HLISCGFMQV SSILADSENA
DETIIRGEAC RLVVATKDYG REFIKQMESI CTMISLGVGV GLDVSTVPLN GYKKNGHIHG
GFFAVTKKLD SCNYLSIYER KPKIALYLSI HNDSIYEAFD LRHPAKEHVE NVFFGVMIND
YFMKCLRKKQ PWYLFPGNVT LNGQNLSDFK NEEYEIMYKR FVAAKLYTKM TTAQELMDRL
LTSLCESGSP YVIWDDIVNR YSNHSHLGKI KTLNLCAEIT NYSSPKESSS CTLLSMNCAM
FKDFPLISEA IYSYLQKVDT VFDKHISSYD NTEECKFTYM LGYMGTRALN DFMGKDRKNR
EIGINPMGVY DMAIINDKNP IDIVGEISEA MYLGCIRASC EYFQQYNVKC NRFDGSHFND
GVPQWMLRDT TTHIEWPEYV YKMMRSGMAN SMLTSQAPTA TTSMLCGVTE SVMIPLNIIT
SKESENGRNA LISYGIMHFI LNRCDETFIL DDDIDTQIAM YAKSAPFIDQ SQSTMFSIEL
NKNTKQTLFD LLKKTYFAEL KTAIYYIMPK SLNPTLSIIR STTKMHQKHY KQKSNDTNIV
ENKNANITDD DDDDDDTLDS DIKTQFKTDK SNPFKRDDCE SCAL
//
