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Database: UniProt
Entry: O58259_PYRHO
LinkDB: O58259_PYRHO
Original site: O58259_PYRHO 
ID   O58259_PYRHO            Unreviewed;       173 AA.
AC   O58259;
DT   01-AUG-1998, integrated into UniProtKB/TrEMBL.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   SubName: Full=173aa long hypothetical molybdenum cofactor biosynthesis protein {ECO:0000313|EMBL:BAA29611.1};
GN   OrderedLocusNames=PH0523 {ECO:0000313|EMBL:BAA29611.1};
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601 {ECO:0000313|EMBL:BAA29611.1, ECO:0000313|Proteomes:UP000000752};
RN   [1] {ECO:0000313|EMBL:BAA29611.1, ECO:0000313|Proteomes:UP000000752}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3
RC   {ECO:0000313|Proteomes:UP000000752};
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Nakamura Y.,
RA   Robb T.F., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
CC   -!- SIMILARITY: Belongs to the MoaB/Mog family.
CC       {ECO:0000256|ARBA:ARBA00006112}.
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DR   EMBL; BA000001; BAA29611.1; -; Genomic_DNA.
DR   PIR; F71165; F71165.
DR   AlphaFoldDB; O58259; -.
DR   STRING; 70601.gene:9377457; -.
DR   EnsemblBacteria; BAA29611; BAA29611; BAA29611.
DR   KEGG; pho:PH0523; -.
DR   eggNOG; arCOG00214; Archaea.
DR   Proteomes; UP000000752; Chromosome.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd00886; MogA_MoaB; 1.
DR   Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR   InterPro; IPR012245; MoaB.
DR   InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR   InterPro; IPR001453; MoaB/Mog_dom.
DR   InterPro; IPR008284; MoCF_biosynth_CS.
DR   NCBIfam; TIGR00177; molyb_syn; 1.
DR   PANTHER; PTHR43232; MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN B; 1.
DR   PANTHER; PTHR43232:SF2; MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN B; 1.
DR   Pfam; PF00994; MoCF_biosynth; 1.
DR   PIRSF; PIRSF006443; MoaB; 1.
DR   SMART; SM00852; MoCF_biosynth; 1.
DR   SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 1.
DR   PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1.
PE   3: Inferred from homology;
KW   Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150}.
FT   DOMAIN          21..167
FT                   /note="MoaB/Mog"
FT                   /evidence="ECO:0000259|SMART:SM00852"
SQ   SEQUENCE   173 AA;  19111 MW;  DB4ED8F0CE7F65C2 CRC64;
     MVSKMGVEEH RREAPKTFKF GVITVSDKGS KGEREDKSGP LIIEELSKLG EHVYYKIVPD
     DKIEILIALF EAIKSGADVV VTTGGTGITR RDVTIESIKP LFDKELSFGE MFRVKSYEEV
     GYAAVLTRAT AGVIRGQERS VIVFSLPGSV NAVKTGLEII KSEVYHILKH ARE
//
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