ID A0A0Y0ABW1_9ALPH Unreviewed; 329 AA.
AC A0A0Y0ABW1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274};
GN Name=UL40 {ECO:0000313|EMBL:AMB17037.1};
OS Macropodid alphaherpesvirus 1.
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus;
OC Simplexvirus macropodidalpha1.
OX NCBI_TaxID=137443 {ECO:0000313|EMBL:AMB17037.1, ECO:0000313|Proteomes:UP000169848};
RN [1] {ECO:0000313|EMBL:AMB17037.1, ECO:0000313|Proteomes:UP000169848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MaHV1.3076/08 {ECO:0000313|EMBL:AMB17037.1};
RX PubMed=26800886; DOI=10.1186/s12864-016-2390-2;
RA Vaz P.K., Mahony T.J., Hartley C.A., Fowler E.V., Ficorilli N., Lee S.W.,
RA Gilkerson J.R., Browning G.F., Devlin J.M.;
RT "The first genome sequence of a metatherian herpesvirus: Macropodid
RT herpesvirus 1.";
RL BMC Genomics 17:70-70(2016).
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC chain family. {ECO:0000256|ARBA:ARBA00009303}.
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DR EMBL; KT594769; AMB17037.1; -; Genomic_DNA.
DR RefSeq; YP_009227273.1; NC_029132.1.
DR GeneID; 26828048; -.
DR KEGG; vg:26828048; -.
DR OrthoDB; 4477at10239; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000169848; Genome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
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 Iron {ECO:0000256|ARBA:ARBA00023004};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000169848};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 169..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 329 AA; 37597 MW; 4936F357B1AFFCB5 CRC64;
MTTKAIKSSS APTAPRVPDS KGLFKYFYTP QCPEINRLRT LSVANRWLES EFVFVGDEAD
VLRLSREELD FYRFLFTFLA AADDLVAEEL GDLAKCFLQK DIAHYYSEQE NIEVVHSRTY
SIIQLVLFNN DAEAREKYVL DNIDHPSIRT KVAWINSRVR ECDTLPGKLL FMILIEGIFF
AASFAAIAFL RTNNLLRVTC QTNDLISRDE AIHTTASCTL YNLHVSDHLK PPPDYITRLF
KEAVDIEIRF IRSRAPSDSS ILDRTALLAI EDYVRFSADR LLGLINMDPI FNVPAPSPDF
PLRLMSVEKH TNFFECRNTA YTGTVTNDL
//
