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Database: UniProt
Entry: A0A177C9G0_9PLEO
LinkDB: A0A177C9G0_9PLEO
Original site: A0A177C9G0_9PLEO 
ID   A0A177C9G0_9PLEO        Unreviewed;       553 AA.
AC   A0A177C9G0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=MOSC domain-containing protein {ECO:0000313|EMBL:OAG04205.1};
GN   ORFNames=CC84DRAFT_1166302 {ECO:0000313|EMBL:OAG04205.1};
OS   Paraphaeosphaeria sporulosa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC   Paraphaeosphaeria.
OX   NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG04205.1, ECO:0000313|Proteomes:UP000077069};
RN   [1] {ECO:0000313|EMBL:OAG04205.1, ECO:0000313|Proteomes:UP000077069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG04205.1,
RC   ECO:0000313|Proteomes:UP000077069};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KV441554; OAG04205.1; -; Genomic_DNA.
DR   RefSeq; XP_018034570.1; XM_018178926.1.
DR   AlphaFoldDB; A0A177C9G0; -.
DR   STRING; 1460663.A0A177C9G0; -.
DR   GeneID; 28762412; -.
DR   InParanoid; A0A177C9G0; -.
DR   OrthoDB; 1781076at2759; -.
DR   Proteomes; UP000077069; 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:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   CDD; cd00207; fer2; 1.
DR   CDD; cd06185; PDR_like; 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; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR005302; MoCF_Sase_C.
DR   InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR30212:SF2; PROTEIN YIIM; 1.
DR   PANTHER; PTHR30212; UNCHARACTERIZED; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF03473; MOSC; 1.
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; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077069}.
FT   DOMAIN          40..185
FT                   /note="MOSC"
FT                   /evidence="ECO:0000259|PROSITE:PS51340"
FT   DOMAIN          244..346
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          467..553
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   553 AA;  61161 MW;  0FD03A171F2BF735 CRC64;
     MVGPIVDLDA PLERDTIVEV RHGKMKPMPG LTIESDIDKS IVDGPIWVSK TGIDGDEHDM
     TFHGGPTKAV HAYCSAHYTS WQTSHPSTAP RFTPGAFGEN LVFVHLNERN VCIGDIFAVG
     PSAPSSTSAT LTLQVSQPRQ PCFKLNHRFG LKNFAPETTR LSRTGWYFRV LEEGWVENGM
     EIRLVDRKYA EWTLERLQGV LYRGAEGAAE MQFLLGVEEL TDEIKGVVRR RLTKLEGATK
     KKEVLWTDWK VVDKVQQTRR ITSFSFAAVH DKVDATPEAG SHVKLRLPNG LVRAYSIVHG
     SRGRFALGIA RDENSRGGSK YLHEHVSVGD ILQIGSITPG IKPNAMASNH VFIVAGIGIT
     AFLWLVEEMV GVNWNVQVHY AVRSAEEMPF RTQLEKLGSR AVVYDKSKGE RMDVESVIKG
     MPWNSQVYVC GPRRLMDDAV KAAQDTGLGE KDVHFEAFGA DVGGDPFEVV IRDKEDRTVL
     VTEEETLLEV LQREFGDVVG SSCEVGNCGT CKVKLRCGKV DHRGTALSAE EKKSEMLSCV
     SRGVGKIEIE IGE
//
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