ID A0A3E2H7D8_SCYLI Unreviewed; 1405 AA.
AC A0A3E2H7D8;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
DE Flags: Fragment;
GN ORFNames=B7463_g7051 {ECO:0000313|EMBL:RFU29315.1};
OS Scytalidium lignicola (Hyphomycete).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Scytalidium.
OX NCBI_TaxID=5539 {ECO:0000313|EMBL:RFU29315.1, ECO:0000313|Proteomes:UP000258309};
RN [1] {ECO:0000313|EMBL:RFU29315.1, ECO:0000313|Proteomes:UP000258309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105466 {ECO:0000313|EMBL:RFU29315.1,
RC ECO:0000313|Proteomes:UP000258309};
RA Buettner E., Gebauer A.M., Hofrichter M., Liers C., Kellner H.;
RT "Draft genome sequence of Scytalidium lignicola DSM 105466, a ubiquitous
RT saprotrophic fungus.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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:RFU29315.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NCSJ02000133; RFU29315.1; -; Genomic_DNA.
DR STRING; 5539.A0A3E2H7D8; -.
DR OMA; LLHASWG; -.
DR Proteomes; UP000258309; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd05195; enoyl_red; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR43775:SF29; ASPERFURANONE POLYKETIDE SYNTHASE AFOG-RELATED; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF13489; Methyltransf_23; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000258309}.
FT DOMAIN 1324..1401
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RFU29315.1"
FT NON_TER 1405
FT /evidence="ECO:0000313|EMBL:RFU29315.1"
SQ SEQUENCE 1405 AA; 154121 MW; 91B28A792975302A CRC64;
MKELDAELEY ASLGRGGTLY GPSFRSMRKI WEGPSWSVME TELRDLDLSL PGPFGSPITV
DPPTLDSHLQ GIGPFQGRAA YMPNYVSRLR ISNKIPAVDK QRFTIVTRMR SHDTRGGKLC
TSVAVFAQCG GSLVPISEWE SVTYRSISSS DTSDLASSLP AGYFWDLIPS MDFACDEDLV
KMVSVDLNEL EIARQKRRKV NSAGVYYMYL ALKETAGDDF SQLPSHLARY LNWSRKVVAR
EHLDFHDEPS SLLAEVSNSD AQGEMLCALG KQLVPILHGA VQPLEIMLKD NLLMRNYEQE
AAITHCSQAL GRFVRSLSDI KPDLSILEIG AGTASATLPV LEELSRGAEE LPAFLNYPLT
YQLASLRMLA RTPQGFAAEH FDVVIASNVL HATPNIATTL EHVRTLLKPN GKLLLIEATR
HAPLCLPFAL LPGWWLSEDQ YRNHEEGPLL SEESWQHVLL AKGFSGVDAK MADYHGGLEH
VMSVMCSSRI GIEQASYNAG SITICGLLTD QEDDEFAQMV SDHVAQHLGC RSSVKPLFEI
DAADDPFCIF IDPPRHSVMR DLSSETFETL KNTLLQTTGL LWVVPDNCHP EAESISGLLR
TMRHETESRN LLFLRDTPCT SEGALAITQV ARRLRDLELA GAAGIRDQDF VWLSGKIQVP
RLRQLTRARD VFASEAGIVV RKMQNIGQGD DSLEMTVDAA GSPDYMYFRK NDVKTRPLGS
DEVLIRVEAT GVNFRDLLLV LGSIPWTKPG FEGAGVVVQT GSGVTDVQPG DRVFYGSLAG
GAFGTYVRIP SWRACKIPDG MSSADAASIA VAYSTAIFAI MRVGRLKKGE TVLIHAASGA
VGQACIVLAQ HIGACVFATA GTPAKREFLH EIFGIPMEHI FSSRTPEFRD GILNATDSRG
VDVIVNCLSG NLLQETWALI ADFGRFVEIG KRDFLQNSYL GMRPFDRNVT FSGVDLRTLF
NQRPEEEREC LQDLVNLLQR KVIVSIRPVS TISISQLATG LRKLQAGQNI GKIVATIGQD
DSVLAESPPV LDVPPGQLLR SDAIYLITGG TGGIGRSLAS WMVENGARNV VLLGRSGSSR
PEVRKLLEEY EGTNVHMRAI TCDVGSRTEL VSALQSIQDL PPVRGIVHGA LYLRDSPLEN
ATFDDWQNIT RPRVQGAWNL HELLEGVDFF ISLSLFVGAV GNVGQGIYAS TTTFFDAFTR
YRIARGLPSA AIALPVVLDV GYAVEKGLTE ALKVSLGATL TEADLHTTIK GAIIGPSSGL
IHDGAAISFR FASGEDPNAL GWKYYHPHAL AERVNAKQRY SEKESWAQRL DERSNGQRAT
NNGDTLLSLL EVLMDKVFSI TMIERDEVEP DAPLSNYSLD SLVSVELRNW IRRQTGVELA
LPEIVGSANL RALATHIFSQ REAKK
//
