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Database: UniProt
Entry: D2S228_HALTV
LinkDB: D2S228_HALTV
Original site: D2S228_HALTV 
ID   D2S228_HALTV            Unreviewed;       163 AA.
AC   D2S228;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=MOSC domain containing protein {ECO:0000313|EMBL:ADB63425.1};
GN   OrderedLocusNames=Htur_4639 {ECO:0000313|EMBL:ADB63425.1};
OS   Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS   13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OG   Plasmid pHTUR02 {ECO:0000313|EMBL:ADB63425.1,
OG   ECO:0000313|Proteomes:UP000001903}.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Haloterrigena.
OX   NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB63425.1, ECO:0000313|Proteomes:UP000001903};
RN   [1] {ECO:0000313|EMBL:ADB63425.1, ECO:0000313|Proteomes:UP000001903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 /
RC   4k {ECO:0000313|Proteomes:UP000001903};
RC   PLASMID=pHTUR02 {ECO:0000313|EMBL:ADB63425.1,
RC   ECO:0000313|Proteomes:UP000001903};
RX   PubMed=21304683; DOI=10.4056/sigs.681272;
RA   Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A.,
RA   Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA   Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Haloterrigena turkmenica type strain (4k).";
RL   Stand. Genomic Sci. 2:107-116(2010).
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DR   EMBL; CP001862; ADB63425.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2S228; -.
DR   KEGG; htu:Htur_4639; -.
DR   HOGENOM; CLU_104911_0_0_2; -.
DR   OrthoDB; 68158at2157; -.
DR   Proteomes; UP000001903; Plasmid pHTUR02.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   Gene3D; 2.40.33.20; PK beta-barrel domain-like; 1.
DR   InterPro; IPR005302; MoCF_Sase_C.
DR   InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR   PANTHER; PTHR36930; METAL-SULFUR CLUSTER BIOSYNTHESIS PROTEINS YUAD-RELATED; 1.
DR   PANTHER; PTHR36930:SF1; MOSC DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF03473; MOSC; 1.
DR   SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR   PROSITE; PS51340; MOSC; 1.
PE   4: Predicted;
KW   Plasmid {ECO:0000313|EMBL:ADB63425.1}.
FT   DOMAIN          21..162
FT                   /note="MOSC"
FT                   /evidence="ECO:0000259|PROSITE:PS51340"
SQ   SEQUENCE   163 AA;  18263 MW;  B8B4580BA7F4CF58 CRC64;
     MTGSGTVERI FIAPEAEAKM EEQTDVEAVA GQGLRGDRYF SEIETGTFVE WEPDEERHDG
     YDLTLIEQEA VTAIEREAGI ELVPGEHRRN IETRDVALNH LVGQRFRVGD VICRGDRLCE
     PCNHLQRITQ DGVLQALTHR GGLRADILED GMIRPGDVIE PLE
//
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