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Database: UniProt
Entry: A0A1V6T7H9_9EURO
LinkDB: A0A1V6T7H9_9EURO
Original site: A0A1V6T7H9_9EURO 
ID   A0A1V6T7H9_9EURO        Unreviewed;      1081 AA.
AC   A0A1V6T7H9;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Carrier domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PENSTE_c010G09530 {ECO:0000313|EMBL:OQE22302.1};
OS   Penicillium steckii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=303698 {ECO:0000313|EMBL:OQE22302.1, ECO:0000313|Proteomes:UP000191285};
RN   [1] {ECO:0000313|Proteomes:UP000191285}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 24891 {ECO:0000313|Proteomes:UP000191285};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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:OQE22302.1}.
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DR   EMBL; MLKD01000010; OQE22302.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6T7H9; -.
DR   STRING; 303698.A0A1V6T7H9; -.
DR   OrthoDB; 2230730at2759; -.
DR   Proteomes; UP000191285; Unassembled WGS sequence.
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; 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   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.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000191285}.
FT   DOMAIN          108..379
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          588..656
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|Pfam:PF00550"
FT   DOMAIN          702..943
FT                   /note="Thioester reductase (TE)"
FT                   /evidence="ECO:0000259|Pfam:PF07993"
FT   REGION          404..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        407..425
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1081 AA;  120317 MW;  229B2053C0FDE374 CRC64;
     MATLTQTATT VGVQTSPSKA DIANRLLNGT LHAAYPPIEQ FLTIDGLLKS HAAQPDEARK
     PLICYPIQGA DDFEEHTAGD LDRYTDVAVQ YYMKQGLGPA DPTLDEAPVI AMLAGSSFEV
     VLTFFALNRL GYAVLFLSTR LTAPAYARLL DMANCNQMIH LQQYDSVARD IFAERSGCTS
     YSMLLRNDWF KQPAVTPIER SGVNQEKEGK KIAWILHSSG STGFPKPIFL TNLQTIANWR
     KSFALRLFTI SPLFHSHALM ELGRAFYTRA PAYLGNHSLP VTYQNLYDAL QVAKPQQISA
     VPYVIKLLAE KPEGIQALAK AQLVLYGGSS CPDDLGDRLV SQGVNLVGNY GATETGQIMT
     SFRPPHDNDW QYMRLHRPVA DYTLMDEISP GVFECVALDG LPSKGPSNSK PPFSSKNPEN
     SFRTSDLFTR HPDPKKTNYY KYLSRLDDRI TLVNGEKVLP IPIEGRIREE ELVGECVVFG
     FQRTVPGALI FRAPEKATHL NNDQFLEVIW PAVEAANARA ETFSRIPKEL VVVKDADVAY
     PKTDKGTCIR AQVYQVFEND IKNAYDNFEG TNQKKGDLAL DIPELENWLL ARFREDLGVE
     LANSETDIFG AGVDSLQTTQ VWRYIVRDLD LGDHTDNLSQ NIVFEKGTVQ ELAKHLFHLR
     TGQKFEQKDE LQVMKELIED YSTFTQHYST ITRQPESEVV IVTGATGNLG AFIVKELLKR
     SNISEVWALV RASGQASAGA RLWKALKDRK ISLTDEEAAK IHAVPSDLSQ SNLGLEGYVL
     DHLLSTTTSV VHSAWAVNFN LGVRSFEQQH IRGTYNLINF CLRSKLPSPA RFFFCSSVSA
     ASATPKPASI PETAVEKLEH AQHIGYGRSK LVTEHITRNA MRKTGMYSRV LRVGQLGGDT
     VSAQWNETEA IALMFRSTLT TGALPELNER PTWLPVDQCA KAISDLALDM DNAKSSDADL
     VYHLVNPHSF SWKNDLLPAL KQGSALPDFE IVSPQEWLKR LANSDSNPET NPSIKLMDFW
     RGKYENHAAP NTGDDQGPVG LSFETACTVR DCPSLGEVKD PVAEGLIQRY IEVWMESWKQ
     T
//
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