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.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//