ID S2YZB1_9ACTN Unreviewed; 584 AA.
AC S2YZB1;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=MOSC domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF1211_03448 {ECO:0000313|EMBL:EPD63107.1};
OS Streptomyces sp. HGB0020.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1078086 {ECO:0000313|EMBL:EPD63107.1, ECO:0000313|Proteomes:UP000014410};
RN [1] {ECO:0000313|EMBL:EPD63107.1, ECO:0000313|Proteomes:UP000014410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGB0020 {ECO:0000313|EMBL:EPD63107.1,
RC ECO:0000313|Proteomes:UP000014410};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., Dover J.,
RA Kim K., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Streptomyces sp. HGB0020.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPD63107.1}.
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DR EMBL; AGER01000013; EPD63107.1; -; Genomic_DNA.
DR RefSeq; WP_016433401.1; NZ_KE150427.1.
DR AlphaFoldDB; S2YZB1; -.
DR STRING; 1078086.HMPREF1211_03448; -.
DR PATRIC; fig|1078086.3.peg.3492; -.
DR HOGENOM; CLU_033218_0_0_11; -.
DR OrthoDB; 9801223at2; -.
DR Proteomes; UP000014410; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06184; flavohem_like_fad_nad_binding; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.33.20; PK beta-barrel domain-like; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR005302; MoCF_Sase_C.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR005163; YiiM-like_3-alpha_domain.
DR PANTHER; PTHR30212:SF2; PROTEIN YIIM; 1.
DR PANTHER; PTHR30212; UNCHARACTERIZED; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF03473; MOSC; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF03475; YiiM_3-alpha; 1.
DR PRINTS; PR00410; PHEHYDRXLASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS51340; MOSC; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Reference proteome {ECO:0000313|Proteomes:UP000014410}.
FT DOMAIN 29..164
FT /note="MOSC"
FT /evidence="ECO:0000259|PROSITE:PS51340"
FT DOMAIN 236..340
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 482..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 61803 MW; FB246C89DBF31C25 CRC64;
MPSLLSVNVG KPKDVAWQGR TVHTGVWKHP VSGPAMVRRL NIDGDGQGDT NGHGGEQRAV
LVYQIESYRY WQRHFGRDDF TFGQFGENLT VDGLPDDEVC IGDRYRIGEA EFEVTQPRVT
CYRVGMRMGE PELPALLVSH HRPGFYMRVL REGHIEAGDR IVRTRTGPGA LTVADTDALL
YLPDRDPAKL RLAVDIPALS PGWQGSFRDL LADGTGGADG ADGAGAAGGV ARPAWDGFRE
LRVADVVAES TTVTSIHLTA TDGTRLPAAR AGQYLTLRIP GAGQPAPVRS YSLSSAPDTG
SYRISVKHEP HGAASGYLTT GLRAGGVLEV AAPRGDFVLT EGAGPVLLIS AGIGVTPTLS
MLHALAAARS DREIWWIHGA RGPREHPLAA EARTLLASLP HSREHVFYSA ATAEERDRHG
ASAGRLTKDE LTALKVPADA TAYICGPTAF MTDMTDALVA AGIDPARVHT ELFGALPAIN
PGLTGRTARP PHQPPGPPGT GPTVTFARSG ISTPFPDGGG SVLELADACD VPARWSCRTG
VCHTCVTPLL SGRVTYEPAP LEPPADGDVL ICCARPGSDI VLDM
//
