ID B6QB72_TALMQ Unreviewed; 780 AA.
AC B6QB72;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Monooxygenase, putative {ECO:0000313|EMBL:EEA26381.1};
GN ORFNames=PMAA_074530 {ECO:0000313|EMBL:EEA26381.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA26381.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
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DR EMBL; DS995900; EEA26381.1; -; Genomic_DNA.
DR RefSeq; XP_002146928.1; XM_002146892.1.
DR AlphaFoldDB; B6QB72; -.
DR STRING; 441960.B6QB72; -.
DR VEuPathDB; FungiDB:PMAA_074530; -.
DR HOGENOM; CLU_009665_12_0_1; -.
DR OrthoDB; 2332834at2759; -.
DR PhylomeDB; B6QB72; -.
DR Proteomes; UP000001294; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR47356:SF2; FAD-BINDING DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR47356; FAD-DEPENDENT MONOOXYGENASE ASQG-RELATED; 1.
DR Pfam; PF01494; FAD_binding_3; 2.
DR PRINTS; PR00420; RNGMNOXGNASE.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Monooxygenase {ECO:0000313|EMBL:EEA26381.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001294};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 453..470
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 504..522
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 534..557
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 577..601
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 613..635
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 664..684
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..174
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 284..339
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 780 AA; 88765 MW; BBE862130D3E2613 CRC64;
MPTEKPFKVL IAGGGIAGLA LAHMLEKFHI DYLLLESHSE IDPTLGASIG IGPHGSRILD
QLDLYEPIAE LDYKDKRGNH IHKENGDCLL NVSRFNHHLE YRHGYPIIFI DRQLFLRVLY
DRLRYKNCVL LNKKVDRVEL LESGVEVITT DGQIVRGSLI IGADGVHSAV RREMYRIASE
QAPEYFAADE QEPVSCHYIC NFGIAQNVAG WIHGHTYTTV GKGYSQLVVS GPGNRIYWFF
FERLPETKYG KDVPRCIREM EAEFIKKHKH APITKTVTFG QIYAKRLFTT LTPLHEYVHE
KWFFDRIFMM GDSAHKLNPI SGQGGNAAIE SAADFVNILL KKKYSRTEGL SGMTSKDIAA
IFTEAQASRY ERAEQIVAYA HLQQSLTAYE KPLISKLTWE YLMPSKGPYG LIDMFSDQFI
DSARLKYLSV KKRARVLPYA DELPSSPLKR VRLIQIVFTL WMVYSAFMAY ELSQSQKPRT
DGLATQNNRF LSLSMQSSPE NRVLQNYYFL SNLISPILIY IIEGYRLGTR NTILALPSLF
LLAIGFKGIA LISPIYAALS VFWSTPLPTR RFVKLGVAHA LIPALILGYV LPTALILSGT
LDIAKWATWA PRVYKFAPVF VGGLAFFFAY LGQIWNSRYQ TPKDQEQSEF ECYKAQDVPT
LKSAYLFAFF LQAMVHITLL AFAYNELRTV AFQSYWNSNH KTIHQAIDLF WSDPEIAFAT
WLISNIYSIW DLRCFGYIKT RDCIIGALNV VAGQLLVGPG ATWAALWYWR EGVIVDLQRN
//
