ID A0A084QZF1_STAC4 Unreviewed; 1077 AA.
AC A0A084QZF1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN ORFNames=S40285_07611 {ECO:0000313|EMBL:KFA69336.1};
OS Stachybotrys chlorohalonata (strain IBT 40285).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA69336.1, ECO:0000313|Proteomes:UP000028524};
RN [1] {ECO:0000313|EMBL:KFA69336.1, ECO:0000313|Proteomes:UP000028524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA69336.1,
RC ECO:0000313|Proteomes:UP000028524};
RX PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT the toxigenic black mold Stachybotrys.";
RL BMC Genomics 15:590-590(2014).
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DR EMBL; KL659535; KFA69336.1; -; Genomic_DNA.
DR STRING; 1283841.A0A084QZF1; -.
DR HOGENOM; CLU_002220_2_1_1; -.
DR InParanoid; A0A084QZF1; -.
DR OMA; YDWKYFR; -.
DR OrthoDB; 2230730at2759; -.
DR Proteomes; UP000028524; Unassembled WGS sequence.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR PANTHER; PTHR43439:SF2; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR PANTHER; PTHR43439; PHENYLACETATE-COENZYME A LIGASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000028524}.
FT DOMAIN 581..668
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1077 AA; 114805 MW; F3630DC8267B0D8A CRC64;
MGSLGATTIR PFVKAPSDFK SPTRQEGAVH TLPELVDFNA VHNADHPFCI QGKAGGLADT
FTHADFKVAV ANCAAWLKQN LPLGPSVVPN AITKNAPVAL FMESDFGLVV HEFALLSLGV
PVSXXXXXXX XXXXXXXXXX XXXVRLAPNA IMHLLKSTGA TSFIVSQRLS GPAKGALGAL
NAAGIATFVG NPYSTWVEPG ADVASKGTFE VPQVLDDITL LLHSSGTTGL PKPIPISHRM
LMFSVSTAGF DTEEEAQGLN VSSLPLFHGF GLVAPGISMA VGKTTVYPAS DGIPNILAII
ELIKRTNARS LMTVPFLLDD VVNNEEGLKV LAGLDFVGTG GAALGAGVGD KLAKAGVKLL
NFYGTTETGP LSLVMVPKNG YDWKYFRLRT DMNYTIDEIE PKDGRKRYRL TVNAFGDAEG
FTIADQLIRN DDFPETDFAA VGRDDDIIIL ATGEKANPLI LETMLTESPL CKVAIAFGEN
QFNLGVIVEP AQPLPEGGEE AFKDSIWPTI VAAGQKTDAY SVIPSKEAII VVPNGVVVPR
TDKGSIARKE VYALFSEEQK AVYEKLAKAV GGEDLKPLNL ETLEADLRAL VIEHSGLKVA
EADLTAETSL FDLGLDSLQA LKLRRVLTAA AGKTEALKDA DLNKIIPPEF VYLNPSVAQM
AASLKNPSGA GAVQAPDPNA FKGVYKFAED FALAGTATEE KGPSAKDNLV VVLTGSSGSL
GSHVLSSLAK NPKVRKVVAL TRKGAGAFDR APFEKRGITL TEEEWSKVAN LEVDPTAEGL
GLNPMAYGFV QSTVTHIVHA AWPMNYLTTL PAFTYQFQFL RNLLQLATGG EFANKRRFIF
ISSIAAVARL SLSNGGSLIR ETPVKPEEAA NGIGYADGKL VCEKVLEAAA VSHAGSLEVT
SVRCGQMTGS RASGAWNEDE QIPMIFRTAQ NLGTLPYLPG TLSWIPVDDA ASVVSDIIFY
EGSLPIVQHL ENPVRQAWAD VIGGVGKLLR IQKPPVPWSE WLDLVAAADD GPGDKFPVKK
LYAFFKFSFP AVATGQVILD TAVARSTSPT LAGLGALDPP TIMRYIAHWQ NIGYLKI
//