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Database: UniProt
Entry: A0A068RP75_9FUNG
LinkDB: A0A068RP75_9FUNG
Original site: A0A068RP75_9FUNG 
ID   A0A068RP75_9FUNG        Unreviewed;       556 AA.
AC   A0A068RP75;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Pyridine nucleotidedisulfide oxidoreductasedomain containing protein {ECO:0000313|EMBL:CDH51427.1};
GN   ORFNames=LCOR_03031.1 {ECO:0000313|EMBL:CDH51427.1};
OS   Lichtheimia corymbifera JMRC:FSU:9682.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX   NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH51427.1, ECO:0000313|Proteomes:UP000027586};
RN   [1] {ECO:0000313|EMBL:CDH51427.1, ECO:0000313|Proteomes:UP000027586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA   Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA   Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA   Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA   Voigt K.;
RT   "Gene expansion shapes genome architecture in the human pathogen
RT   Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT   terrestrial Mucorales (Mucoromycotina).";
RL   Submitted (AUG-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:CDH51427.1}.
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DR   EMBL; CBTN010000009; CDH51427.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068RP75; -.
DR   STRING; 1263082.A0A068RP75; -.
DR   VEuPathDB; FungiDB:LCOR_03031.1; -.
DR   OrthoDB; 22856at2759; -.
DR   Proteomes; UP000027586; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.100; -; 1.
DR   Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016137; RGS.
DR   InterPro; IPR036305; RGS_sf.
DR   InterPro; IPR044926; RGS_subdomain_2.
DR   PANTHER; PTHR43735; APOPTOSIS-INDUCING FACTOR 1; 1.
DR   PANTHER; PTHR43735:SF3; FERROPTOSIS SUPPRESSOR PROTEIN 1; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF00615; RGS; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR   PROSITE; PS50132; RGS; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027586}.
FT   DOMAIN          1..65
FT                   /note="RGS"
FT                   /evidence="ECO:0000259|PROSITE:PS50132"
SQ   SEQUENCE   556 AA;  62915 MW;  299082B5CBD31912 CRC64;
     MQSLLSDPKL LQEFKTFLDE HSHGDELKND LIFVEAMTQL HHESDSKKIE SLMHRIYKTF
     LAPDATLPLT HVSTGKQVKR DLRSLAWSIL GQEDVTDVLK DTEDQVETKM MHMIKEFEQY
     KGMNIRQSLE PTEELQPYKV RVVIVGGGFT GFTVASILDR MPLFHVTLID TKACFEYTPG
     IVKRIVHPED NESDALRVRH DSYVRNGRVI IGYAEGICNN ATSIRVNGEK IFFEYLLIAT
     GSSYTSDLKS TDPSYIYRLS GLHQVSHDLA KAKRVLIVGG GLVGCELAIE IAETWPEKHI
     TLVESHPILV HRAKQPQQDK VRSFLSDELG VEVVCDERIT DVGEGEYMGT SGRIYKDYDK
     VFMATGTRPQ GRLLLSGSSN LDSCVDSYGR IMVKPTLQID HPEYTHIFAG GDVTNVKEEK
     TGYAATLAGV CIARNICRMC KGKKPLHQGA KGTLPAPDQP LSSLLVDMNE NHRRRKNMDK
     IKKYLGFLNP TWAALKCYDE QEYLQMVQGE SSPMTQPFGR LPRTLCKHPT HRNRFRKSAS
     FLCLDRENLH PNRDCK
//
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