ID C5PIA4_COCP7 Unreviewed; 1143 AA.
AC C5PIA4;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Amine oxidase, flavin-containing family protein {ECO:0000313|EMBL:EER24257.1};
GN ORFNames=CPC735_056270 {ECO:0000313|EMBL:EER24257.1};
OS Coccidioides posadasii (strain C735) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=222929 {ECO:0000313|EMBL:EER24257.1, ECO:0000313|Proteomes:UP000009084};
RN [1] {ECO:0000313|EMBL:EER24257.1, ECO:0000313|Proteomes:UP000009084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C735 {ECO:0000313|Proteomes:UP000009084};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|ARBA:ARBA00005995}.
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:EER24257.1}.
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DR EMBL; ACFW01000049; EER24257.1; -; Genomic_DNA.
DR RefSeq; XP_003066402.1; XM_003066356.1.
DR AlphaFoldDB; C5PIA4; -.
DR GeneID; 9691872; -.
DR KEGG; cpw:CPC735_056270; -.
DR VEuPathDB; FungiDB:CPC735_056270; -.
DR HOGENOM; CLU_004498_1_2_1; -.
DR OrthoDB; 5402444at2759; -.
DR Proteomes; UP000009084; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140993; F:histone modifying activity; IEA:UniProt.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0010558; P:negative regulation of macromolecule biosynthetic process; IEA:UniProt.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR PANTHER; PTHR10742:SF386; LYSINE-SPECIFIC HISTONE DEMETHYLASE 1A; 1.
DR Pfam; PF01593; Amino_oxidase; 2.
DR Pfam; PF04433; SWIRM; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF47095; HMG-box; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
DR PROSITE; PS50934; SWIRM; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267}.
FT DOMAIN 200..295
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT DOMAIN 989..1069
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DNA_BIND 989..1069
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 1..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1143 AA; 125688 MW; 3912D8A415281222 CRC64;
MDGSASINAE SSSETVKSVE SEIPPMKTKS SIEVDGGVSG SRDLPAPVAL TKTATSESED
GKMGILTSND GVYGDDRKNE VGSNQLTDMF PLSTSYPEDD SSQGSSELCK ELGRFSESHD
TPNGSTTSAS LISPFSTEKS ITPSAQLNQT LNTPPASAPV SAPSSSRKKQ QQPPLSSHTE
ARPRSSIPTR MAPTLYAEQC LAAAYASRLN PYALHKDEQE ILQDSLCHLH VTTYLNIRNG
ILRLWTRNPM LTVTEEEALG CAKDRRWMNL ASVAYDWLVR NGYINFGCVS ISKNPRPTKR
RRRREGPTIV VIGAGMAGLG CARQLESLFQ HYGGDTAPAK VIVLEGRKRI GGRIYSHPLQ
SLKPGTLVPN LRPTAEMGAQ IIVGFDNGNP LDPIIRAQLA LHCHLLRDIS TIYDTDGSPV
DEVHDSLVEK LYNDILNRCG IYRHKAVINK TAGGDRELMH SARDCLLDDG ITIRQYEDAA
ASGTVDLLLP AKRLRRGVGH RTAEIGPTVI SEPVVAPQIS HVEPANGMPA ALTCQAMGWN
LREGASNADT LLLDEVAGAT KTQTLGAVMD EAIRQCHKWL PLTPKDMRLL NWHYANLEYA
NAANLGKLSL AGWDQDMGNE FEGEHAQVIG GYQQVPRGLW SHPSKLDVRP NKVVTKISYK
VNGSPNGKAR IYLDDGEVIT ADKVVLTAPL GVLKSKSITF SPPLPAWKTG AIDRLGFGTM
NKVILVFEKP FWDVERDMIG LLREPAVPES LSQADYASSR GRFYLFWNCM KTSGLPMLIA
LMAGDSAHHA EALPDSEILH EVTSQLRNIF KGTAVPDPLE TIVTRWGQDR FSRGSYSYVA
AESLPGDYDL MAKSTGNLYF AGEATCGTHP ATVHGAYLSG LRVAKEVLES VIGPIKVPTP
LVVSKTKTPS THTPVTPPAA APEQTMINPK KRKEPQSSSV DHPNSTERPA ATPSGQGRPV
YEMAFVEEYR RAISRAIQAE LGDPEKQPRK EPINPFLLFQ KDYWFVCKAR CDEVRRRSTG
NPAAKTPRDE VRQALGQMWR EASEEVRRRY LDQIEINRKI NNEKMSKWKE RITVWERHSA
EIKDRWCAAN PYSKFVKEMD SQKVANAKTS FSDYTSFRLT GATDVGALGF AGRLRFQGRD
DVP
//
