ID J3UIJ5_9CAUD Unreviewed; 477 AA.
AC J3UIJ5;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274};
GN ORFNames=CbK_gp111 {ECO:0000313|EMBL:AFU86943.1};
OS Caulobacter phage phiCbK.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Dolichocephalovirinae; Shapirovirus; Shapirovirus cbk.
OX NCBI_TaxID=2927985 {ECO:0000313|EMBL:AFU86943.1, ECO:0000313|Proteomes:UP000013922};
RN [1] {ECO:0000313|EMBL:AFU86943.1, ECO:0000313|Proteomes:UP000013922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23050599; DOI=10.1186/1471-2164-13-542;
RA Gill J.J., Berry J.D., Russell W.K., Lessor L., Escobar Garcia D.A.,
RA Hernandez D., Kane A., Keene J., Maddox M., Martin R., Mohan S.,
RA Thorn A.M., Russell D.H., Young R.;
RT "The Caulobacter crescentus phage phiCbK: genomics of a canonical phage.";
RL BMC Genomics 13:542-542(2012).
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; JX100813; AFU86943.1; -; Genomic_DNA.
DR RefSeq; YP_006988007.1; NC_019405.1.
DR GeneID; 13994734; -.
DR KEGG; vg:13994734; -.
DR OrthoDB; 4477at10239; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000013922; Genome.
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; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 1.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR011767; GLR_AS.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR012348; RNR-like.
DR InterPro; IPR033909; RNR_small.
DR InterPro; IPR000358; RNR_small_fam.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR23409; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN; 1.
DR PANTHER; PTHR23409:SF18; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M2; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR Pfam; PF00268; Ribonuc_red_sm; 1.
DR SUPFAM; SSF47240; Ferritin-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000013922}.
FT DOMAIN 395..451
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
SQ SEQUENCE 477 AA; 55297 MW; 390CF38A4E98EE90 CRC64;
MSLLKSRDYY KPFVYPWAYE AYKTMQAMHW LPHEAPMDQD IQDWNEKLTP DEKSLLTQLF
RFFTQADVDV ARGYFEKYGP RFPHPEVRMM LGAFIAAEAN HIDAYSTLID TLGLPEVEFR
AFLDYEAMRE KHEYMFNRDS GNSIADLMVD IAVFSAFGEG MQLFSSFALL MSFQRRNRMK
GMTTIVEWSI RDESHHVESM IKLLHELIKE HPRSWNDETK KRIYDACRAM VDLEDAFIDQ
AFAIAPDMSE AKPAAKNRAE RRSGKFRKLQ IEGVTPEDTK QYIRYIADRR LLQLGLKPNY
GVKDNPFDWL DWIMNAPTHT NFFEQRSTEY GKGEIPGWER AFSFLQRPVW TPPLEDDGCA
EEGVCAIPET PRYWSVKRLD EVAVTAPAGA PEYRVYTKAN CPHCDRAKAY LDREGIPYDA
VQPSDEDRRA KFEDVRQNWG HPTWNTSPMI FLLDAAGEEE AFIGGADALA DHLDIPR
//
