GenomeNet

Database: UniProt
Entry: H1V8I2_COLHI
LinkDB: H1V8I2_COLHI
Original site: H1V8I2_COLHI 
ID   H1V8I2_COLHI            Unreviewed;       530 AA.
AC   H1V8I2;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=MOSC domain-containing protein {ECO:0000313|EMBL:CCF36535.1};
GN   ORFNames=CH063_01513 {ECO:0000313|EMBL:CCF36535.1};
OS   Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum destructivum species complex.
OX   NCBI_TaxID=759273 {ECO:0000313|EMBL:CCF36535.1, ECO:0000313|Proteomes:UP000007174};
RN   [1] {ECO:0000313|Proteomes:UP000007174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174};
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
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; CACQ02002024; CCF36535.1; -; Genomic_DNA.
DR   AlphaFoldDB; H1V8I2; -.
DR   STRING; 759273.H1V8I2; -.
DR   EnsemblFungi; CCF36535; CCF36535; CH063_01513.
DR   VEuPathDB; FungiDB:CH63R_08982; -.
DR   eggNOG; ENOG502SEJJ; Eukaryota.
DR   HOGENOM; CLU_003827_17_2_1; -.
DR   Proteomes; UP000007174; 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   InterPro; IPR005163; YiiM-like_3-alpha_domain.
DR   PANTHER; PTHR30212:SF2; PROTEIN YIIM; 1.
DR   PANTHER; PTHR30212; UNCHARACTERIZED; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF03473; MOSC; 1.
DR   Pfam; PF03475; YiiM_3-alpha; 1.
DR   PRINTS; PR00409; PHDIOXRDTASE.
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}.
FT   DOMAIN          1..162
FT                   /note="MOSC"
FT                   /evidence="ECO:0000259|PROSITE:PS51340"
FT   DOMAIN          222..333
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          446..530
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   530 AA;  59113 MW;  BA49C7DC6BC1E76E CRC64;
     MSSTQEVDLW SPFTSDILLE VRTGVMTKMP GLEVTSGIDK SLREGPVHVA SLGLELDEHD
     PTFHGGPDKA IHSSDRFKPG AFGENFVTKH MNERNVCIGD IIHVGDEVVL QVSLPRQPCY
     KLNHRFQLKN FAPKTFETSR TGWYYRVLQG GKVKAGDKIR LIERKWPKWT IERIQEYLHR
     NQNDLAMNEE LATIEELGKE CRGAFQRRVA KAQAQEKRVK GDVWRDFKIV KKTTQTPRIS
     SFVLEAVSMR EDPGDLNPGA HAKLKLPNGL LRSYSIVSGD RNKFELGIAL NDSSRGGSRY
     LHESMAVGDV LRVGRITTDV KMSSASSNHV FIVGGIGVTA FLALAEGYHE IHYNFEMHYA
     VRSANDIPFQ SRLEVFGRSV RLYDGSKGER MDVDDIMRTL KWNSHVYVCG PTRLMEAVRK
     AAEQCALDEN DVHYEAFAAD TSGDPFEVEV VNRDGKILKV GEEETLLEVL KREVGGDVAS
     SCEVGNCGTC KVGLKAGRVD HRGTALTSTD KVESMLSCVS RGIGRISIEI
//
DBGET integrated database retrieval system