ID RIR2_HHV1K Reviewed; 340 AA.
AC P06474;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 30-NOV-2016, entry version 94.
DE RecName: Full=Ribonucleoside-diphosphate reductase small subunit {ECO:0000255|HAMAP-Rule:MF_04028};
DE EC=1.17.4.1 {ECO:0000255|HAMAP-Rule:MF_04028};
DE AltName: Full=Ribonucleotide reductase small subunit {ECO:0000255|HAMAP-Rule:MF_04028};
GN Name=RIR2 {ECO:0000255|HAMAP-Rule:MF_04028}; Synonyms=UL40;
OS Human herpesvirus 1 (strain KOS) (HHV-1) (Human herpes simplex virus
OS 1).
OC Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae;
OC Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10306;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6292456;
RA Draper K.G., Frink R.J., Wagner E.K.;
RT "Detailed characterization of an apparently unspliced beta herpes
RT simplex virus type 1 gene mapping in the interior of another.";
RL J. Virol. 43:1123-1128(1982).
RN [2]
RP SEQUENCE REVISION.
RA Wagner E.K.;
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP REVIEW.
RX PubMed=18990579; DOI=10.1016/j.tibs.2008.09.008;
RA Lembo D., Brune W.;
RT "Tinkering with a viral ribonucleotide reductase.";
RL Trends Biochem. Sci. 34:25-32(2009).
CC -!- FUNCTION: Ribonucleoside-diphosphate reductase holoenzyme provides
CC the precursors necessary for viral DNA synthesis. Allows virus
CC growth in non-dividing cells, as well as reactivation from latency
CC in infected hosts. Catalyzes the biosynthesis of
CC deoxyribonucleotides from the corresponding ribonucleotides.
CC {ECO:0000255|HAMAP-Rule:MF_04028}.
CC -!- CATALYTIC ACTIVITY: 2'-deoxyribonucleoside diphosphate +
CC thioredoxin disulfide + H(2)O = ribonucleoside diphosphate +
CC thioredoxin. {ECO:0000255|HAMAP-Rule:MF_04028}.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04028};
CC -!- PATHWAY: Genetic information processing; DNA replication.
CC {ECO:0000255|HAMAP-Rule:MF_04028}.
CC -!- SUBUNIT: Heterotetramer composed of a homodimer of the large
CC subunit (R1) and a homodimer of the small subunit (R2). Larger
CC multisubunit protein complex are also active, composed of
CC (R1)n(R2)n. {ECO:0000255|HAMAP-Rule:MF_04028}.
CC -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000255|HAMAP-
CC Rule:MF_04028}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04028}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase
CC small chain family. {ECO:0000255|HAMAP-Rule:MF_04028}.
DR EMBL; J02212; AAA66436.1; -; Genomic_DNA.
DR ProteinModelPortal; P06474; -.
DR UniPathway; UPA00326; -.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of 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 GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
DR CDD; cd01049; RNRR2; 1.
DR Gene3D; 1.10.620.20; -; 1.
DR HAMAP; MF_04028; HSV_RIR2; 1.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR012348; RNR-rel.
DR InterPro; IPR033909; RNR_small.
DR InterPro; IPR030475; RNR_small_AS.
DR InterPro; IPR000358; RNR_small_fam.
DR PANTHER; PTHR23409; PTHR23409; 1.
DR Pfam; PF00268; Ribonuc_red_sm; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
DR PROSITE; PS00368; RIBORED_SMALL; 1.
PE 3: Inferred from homology;
KW DNA replication; Host membrane; Iron; Membrane; Metal-binding;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1 340 Ribonucleoside-diphosphate reductase
FT small subunit.
FT /FTId=PRO_0000190504.
FT TRANSMEM 180 200 Helical. {ECO:0000255|HAMAP-
FT Rule:MF_04028}.
FT ACT_SITE 131 131 {ECO:0000255|HAMAP-Rule:MF_04028}.
FT METAL 94 94 Iron 1. {ECO:0000255|HAMAP-
FT Rule:MF_04028}.
FT METAL 124 124 Iron 1. {ECO:0000255|HAMAP-
FT Rule:MF_04028}.
FT METAL 124 124 Iron 2. {ECO:0000255|HAMAP-
FT Rule:MF_04028}.
FT METAL 127 127 Iron 1. {ECO:0000255|HAMAP-
FT Rule:MF_04028}.
FT METAL 187 187 Iron 2. {ECO:0000255|HAMAP-
FT Rule:MF_04028}.
FT METAL 221 221 Iron 2. {ECO:0000255|HAMAP-
FT Rule:MF_04028}.
FT METAL 224 224 Iron 2. {ECO:0000255|HAMAP-
FT Rule:MF_04028}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 123 139 ipat:RIBORED_SMALL [T]
FT MYHIT 34 340 ihamap:HSV_RIR2 [T]
FT MYHIT 40 304 ipfam:Ribonuc_red_sm [T]
SQ SEQUENCE 340 AA; 37966 MW; 921DC04B9D278DE5 CRC64;
MDSAAPALSP ALTAHTGHSA TADLAIQIPK CPDPERYFYT SQCPDINHLR SLSILNRWLE
TELVFVGDEE DVSKLSEGEL SFYRFLFAFL SAADDLVTEN LGGLSGLFEQ KDILHYYVEQ
ECIEVAHSRV YNIIQLVLFH NNDQARREYV AGTINHPAIR AKVDWLEARV RECASVPEKF
ILMILIEGIF FAASFAAIAY LRTNNLLRVT CQSNDLISRD EAVHTTASCY IYNNYLGGHA
KPPPDRVYGL FRQAVEIEIG FIRSQAPTDS HILSPAALAA IENYVRFSAD RLLGLIHMKP
LFSAPPPDAS FPLSLMSTDK HTNFFECRST SYAGAVVNDL
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