ID A0A3D8QK13_9EURO Unreviewed; 1532 AA.
AC A0A3D8QK13;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN ORFNames=DSM5745_10446 {ECO:0000313|EMBL:RDW61774.1};
OS Aspergillus mulundensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1810919 {ECO:0000313|EMBL:RDW61774.1, ECO:0000313|Proteomes:UP000256690};
RN [1] {ECO:0000313|EMBL:RDW61774.1, ECO:0000313|Proteomes:UP000256690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5745 {ECO:0000313|EMBL:RDW61774.1,
RC ECO:0000313|Proteomes:UP000256690};
RX PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA Xiong C., Yue Q., Zhang X.;
RT "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT and Morchella septimelata.";
RL IMA Fungus 9:199-223(2018).
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:RDW61774.1}.
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DR EMBL; PVWQ01000016; RDW61774.1; -; Genomic_DNA.
DR STRING; 1810919.A0A3D8QK13; -.
DR OrthoDB; 2311449at2759; -.
DR Proteomes; UP000256690; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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 CDD; cd19532; C_PKS-NRPS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 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 Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
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; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 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; SSF52777; CoA-dependent acyltransferases; 2.
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:UP000256690}.
FT DOMAIN 1014..1096
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1361..1401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1361..1386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1532 AA; 164370 MW; 00EEE846EDC42AF0 CRC64;
MSLVRPSQPV AVPVPNGKEH PNPEPTVERT VPLSYGQSRF WFLSQLVPDQ TALNITFRAR
LNGPLRYRRL AAAVAAVGRR HEALRTAFAT DAQHGGPMQV VLAASPLSLE YCRVTSEDEV
EKEYRELKAH VYDLETGRTM RIRLLSLSPL VNFLLVGYHH INMDGVSFEV LLGELDLLYK
AGSLPDQALL QYPDYAVRQR AAISSARGTM DEAAAFWRRE LHDAPGALPI LPFAAASASR
PTTPSYSNIR VDARIPASLN SRIRAVAAAN KVSPYTFHLA VYATLLSRLF STTDLIIGVG
DSGRSDPDAR GSIGLFLNIL PLRLRLSNKD PDTDGTPFVH LLKNARRTML AALAHSAYPF
DAILDLVHAS RSSTHNPLFQ AFMNYRSSVN EKRTFAGCEA LGEEYAAGGT AYDITVDVLE
GNESGSLVML SVLEGLYTKD NARVLLEMYM RLLDVFSADV MADVHTVSLF AKDEVERGLR
MGRGSTMRST WPETLIHRVD DITSQSPDVL ALSDGSGAVT YAQMALRTTQ IASVLQHSGI
KRRSLVAMYV EPSADAVCCM LATMRLGAVY VPLDVRSPAS RLATIVTDCM PAALLTDGKS
DAGALGANCP VVSIANLAST TSTVPISTTA TDTAALLYTS GTTGTPKGVK LTHAGLRNLM
EGYVMSYGIT AHNVLQQTAL SFDFSLEQIF TALALGGTLV IVPREKRGDP ASIARTIRES
HVTYAAGTPL ELLSWVQYGA PDLKASDLQV VVAGGEQYTP DLYRALTGLG KGLQLLNIYG
PTEVTVACSK IELTEAEAMG RGRIPAGFTL PNCAVYILDH ALNALPPGYP GEVFIGGAGV
GGYLDDALTA ARFLPDPFAS EFAQSHGWTR MYRTGDRGML RDGALVILGR MDGDTQVKIR
GIRIEVEEVE KAVLQCAGGR LAGVVVTPRG EPPAYLVAHV VFTDQSPGIL PTEEHASFLK
TLRRALPLPE TMRPAVMAPI RALPLNAHGK LDRKSLAALE LDIPPTLDTN GASNILTPAE
AQLRALWERV IPPDILGFHS LSPASDFFQV GGNSMSLVAL HALIRKELDA PSSLTLAALF
QSSSLGKMAD AITGSATTKN GSIAANNDSH TRNMDTDEID WTAETSLPSL SLPAPVHPPR
TIALTGATGF VGRHILRRLL ASPTTQGLHI HCLAVRNPTS LTPFFSHPRP DIKITIHDGD
LASPTLGLSP STFAALSASL DCIIHNGADV SFMKSYASLR AANVTSTKTL IKLAMQAGRA
VPLHYVSSAV VGRLMLAQTS SSSTSNASSP YLDAEFPPVS VSSFPPPPGY SDAYGMTKWA
SEVVLERANK TVGLPVVTHR LSSVTVPAML GPIFTGIPNS NGTARKSQLP VRTVNGNGNG
NVNGTGTEER EDPEGNEEDI PPLDLMHNVL RFSRLLRAVP VSEHWTGSLD FVCVGTVARG
IVREIEKGSP RRGEAGVPVQ FRHHCGDAVV PLTELRALLM DEDAGESEVQ EVPLGQWISR
AREAGMSGLV AAVLEGVEGG EGVLVFQRLR RE
//