ID B6QN70_TALMQ Unreviewed; 891 AA.
AC B6QN70;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Carrier domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PMAA_061530 {ECO:0000313|EMBL:EEA22375.1};
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:EEA22375.1, 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).
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DR EMBL; DS995903; EEA22375.1; -; Genomic_DNA.
DR RefSeq; XP_002150984.1; XM_002150948.1.
DR AlphaFoldDB; B6QN70; -.
DR STRING; 441960.B6QN70; -.
DR VEuPathDB; FungiDB:PMAA_061530; -.
DR HOGENOM; CLU_008054_0_0_1; -.
DR OrthoDB; 2230730at2759; -.
DR PhylomeDB; B6QN70; -.
DR Proteomes; UP000001294; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR PANTHER; PTHR45681:SF6; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45681; POLYKETIDE SYNTHASE 44-RELATED; 1.
DR Pfam; PF18558; HTH_51; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001294};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 112..152
FT /note="Carrier"
FT /evidence="ECO:0000259|Pfam:PF00550"
FT DOMAIN 512..763
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
FT REGION 49..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 891 AA; 99944 MW; ECF0B912DD0F76FF CRC64;
MIGACPSEKE WVSDVFVFDP VEGELVEVIL GIHYIRVARQ GLGKLLSRLT PSSKLPHPSP
QPNAAETPKT NGVHEVRHAF DNMTTEPISE PHSNGANEKS KKELPELDIA GKVRDLICTL
SGLEPDMIKP EADLANLGID SLMGMELARE IEIMFKSAFG FQVHPSAADR EADNHEKPHV
NRFTHPKANG NMNGGSTKVN GTHSHANDPS MPNDMVVPTI AILDAFRETT QLTDQFIEQN
NFGNYVQHTL PRLTKLCVIQ IIDGFEELGC SLRDAHLGQI LNRIKYLPKH EQFVTFFYGV
LEKAGPVDLD GSRMTRTATA VPAESAYTLS QNLALDFPEH TYDSQLTYLT GSKLADYLTG
KADGLQLIFA SAEGRNIVSG MYGKSPINMI DLVFGLLEGW WLFDDGRQHA LVPPSIWKTI
MQSVGYGYVD WTYSNRPEAA IQRIIIALAS SKSRNRVHHP HQLLQRHSTD FTARQAIVDD
FVKKYSSGFA APVVSKALEE GLEGHVDQCI LVTSATGSLG SHLVAYFTKL PNVKRMICVN
RYSPSLDCRI RQRKALESKG LFLNSVELAK IHVLETDTVK PMMALSNLEY TKLINSVTHI
IHNAWPMSIT RSIHTFEQQF KAMRNLIELA RQISCRYHHF HRNGPRVGFQ FISSIATVGC
YPLFSGKARV PEDRMLVDSV MPTGYGEAKL IWETMLDETL HKYPQHFRPM IVRIGQIAGS
EGSGYWNPVE HLAFLIKSSQ TLNILPDLEG DLSWCPVNVV AATLGELLLD EQTWYPVYHI
ENPVRQPRRK MIHMLADDFH IPNTGIIPFK EWLERVRRSP SSPDDNPASN LAGFLDMYFV
RMSCGGLILD TARSRENSWT LRDTGPVSRS LVMKFIQVWK ERGFLKQSVA S
//