ID A0A177CRA2_9PLEO Unreviewed; 439 AA.
AC A0A177CRA2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:OAG09472.1};
GN ORFNames=CC84DRAFT_1234964 {ECO:0000313|EMBL:OAG09472.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG09472.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG09472.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG09472.1,
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 -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
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DR EMBL; KV441549; OAG09472.1; -; Genomic_DNA.
DR RefSeq; XP_018039837.1; XM_018183833.1.
DR AlphaFoldDB; A0A177CRA2; -.
DR STRING; 1460663.A0A177CRA2; -.
DR GeneID; 28767319; -.
DR InParanoid; A0A177CRA2; -.
DR OrthoDB; 1422702at2759; -.
DR Proteomes; UP000077069; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR PANTHER; PTHR13789:SF187; MONOOXYGENASE; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000077069}.
FT DOMAIN 17..44
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 123..377
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 439 AA; 48819 MW; 92D0DD5F946FF9DD CRC64;
MAVPVTNGAK PQTGIRVIIV GAGFGGLTAA IECVRQGHSP IIYESFPSLK ILGDIISFGP
NAGRIFARWE NGDIARAMRK ISIDLQAYGF NIHKWDTGEV VINQKSPPRD ETAPVFNGHR
GELHEIVFNY AKKLGVEIVL DSRVENYWET EDAAGIILGD GTRVEGDVVV GSDGVRSKAR
TLVLGYEDKP KSSGYAVWRS WFSNEDMLAD PETRQFCENG DTFNGWIGPD VHFLFSTLKG
GSDCCWVLTH KDEHDIDESW SFPGKLSEVK DVLRDWDPMC TKIISKTPEE KLVDWKLVYR
DPLPTWVSGY GSAPGHGRIC LLGDSAHPFL PTSAQGATQA LEDGVTLAVL LRKAGKSNIK
GGLRAYQDVR YERVRKVQKT GETTRDMWHN TDWEKVKKDP QSIAFPREDW IFSHDAEKHA
EEVGDEMIAK ASTSVEQQA
//
