ID A0A1V6QCX2_9EURO Unreviewed; 968 AA.
AC A0A1V6QCX2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN ORFNames=PENSOL_c085G10355 {ECO:0000313|EMBL:OQD86847.1};
OS Penicillium solitum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD86847.1, ECO:0000313|Proteomes:UP000191612};
RN [1] {ECO:0000313|Proteomes:UP000191612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
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:OQD86847.1}.
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DR EMBL; MDYO01000085; OQD86847.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6QCX2; -.
DR STRING; 60172.A0A1V6QCX2; -.
DR OrthoDB; 2311449at2759; -.
DR Proteomes; UP000191612; 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 CDD; cd05930; A_NRPS; 1.
DR Gene3D; 3.30.300.30; -; 1.
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; IPR045851; AMP-bd_C_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; PTHR44845:SF6; BETA-ALANINE-ACTIVATING ENZYME; 1.
DR PANTHER; PTHR44845; CARRIER DOMAIN-CONTAINING PROTEIN; 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.
DR PROSITE; PS50075; CARRIER; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Reference proteome {ECO:0000313|Proteomes:UP000191612}.
FT DOMAIN 532..612
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 968 AA; 105389 MW; 7209EA695FAA7B38 CRC64;
MTIVHRLDEV ALRYPDHVAL KPHDGSPLTY AEVQRRINVI ANELLRNGVG TGTRVGVFQS
PSAAWICSLI AILRVGGAYI PLDKKVGINR LAIIMKETQA SVVLVDTNSI SDYALLHTTA
KPIDVWGLND FTARAVRNMA IPSQTAVIMY TSGSTGVPKG IMIAHSAYVH HVQSCSEVWK
LKQGSEIILH QSSYAWDASL WQIMVSLCSG ATLVIASDLT RGDPVAITRL IASENVTCTL
ATPTEYLAWV RHGRSHLSNS RLSTAVCGGE FMSSGLIQEI KNLHRPDLKL INAYGPAEIS
VACSGSEVPY NLLDSTSTSP APALYTLPNY SVYIVDENLK PVPIGVPGEV VVGGAGVAQG
YLDGTKTTER FSNDRYASKL FQERNWTTIY RTGDRGKLNR NGGLILLGRM DGDNQIKLRG
IRINFEEIET TIVSYSAGAI TQAVVSVRSD ATDSATDQFL VAFAIMVPTH DSENALQFLA
RLSQELPLPH HMRPAAIIPV ENIPQNTSGK TDRAAVSALP IPLISSKLPD DSTLTAFEQS
LRQLWQQALP RELSSFHSID SLSDFFHVGG SSLALVNLQA LIKENLGASM ALYQLFEAST
LRGMAARIQD ISRPALELDV NWDTEVEIAS DLTSSLNYSD THIIASGVKT VVLTGATGFL
GKEILRRLIE DEKVSSIHCL AVRKRSLDLP ELFAHPKVHL HFGDLGAPQL GLSESDTRSI
FSCADIVIHN GADVSFMKAY RTLKLINVAS TKELVKLALP RRIPFHFVSS AGVARLAGQE
SFGETSVSSY PPPSRPTDGY IAAKWVSEVY LERINRQFGL PVWIHRPSSI TGTDAPELDL
MGNVMRFTKT TQKVPDSSSW SGVFDLISVQ SAASQLLEAV HQSSVTELAI GSVTYLYESG
ETKIGRDEIM PLMESGSGQQ FQIVSLDEWV NAAEQAGMSV LLGEYLRRAS DGQVLLPRLI
KAGFSEDE
//