ID A0A2V1C9N7_9HELO Unreviewed; 1779 AA.
AC A0A2V1C9N7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
DE Flags: Fragment;
GN ORFNames=DL98DRAFT_386885 {ECO:0000313|EMBL:PVH82351.1};
OS Cadophora sp. DSE1049.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiales incertae sedis; Cadophora.
OX NCBI_TaxID=1485229 {ECO:0000313|EMBL:PVH82351.1, ECO:0000313|Proteomes:UP000244409};
RN [1] {ECO:0000313|EMBL:PVH82351.1, ECO:0000313|Proteomes:UP000244409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE1049 {ECO:0000313|EMBL:PVH82351.1,
RC ECO:0000313|Proteomes:UP000244409};
RX PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT "Comparative genomics provides insights into the lifestyle and reveals
RT functional heterogeneity of dark septate endophytic fungi.";
RL Sci. Rep. 8:6321-6321(2018).
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DR EMBL; KZ804133; PVH82351.1; -; Genomic_DNA.
DR STRING; 1485229.A0A2V1C9N7; -.
DR Proteomes; UP000244409; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR CDD; cd05918; A_NRPS_SidN3_like; 1.
DR CDD; cd19545; FUM14_C_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
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; 2.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000244409}.
FT DOMAIN 541..617
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1355..1429
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PVH82351.1"
FT NON_TER 1779
FT /evidence="ECO:0000313|EMBL:PVH82351.1"
SQ SEQUENCE 1779 AA; 197053 MW; C874DE9053FD8B47 CRC64;
AAQDPPSQAV CSWDGNLTYA ELDEYSSRLA SSLSGKGVAP EVVVPVAFEK SRWAIVSALA
VLKAGGAFLL LDTSQPIARL KSAVEQTGAR LALSSSAFRS NCGQLVEEVI VVENDTISAL
EVGQSLPDVE SSAAAYYIFT SGSTGSPKGV IVEHTQLSTT ALYCGKRIGY DEKPRVFQFA
SYAFDMCITD IFATLAHGGT VCIPSDWERN NDIVGAIRRM EVSSARFTPS LVSNLALEEA
SALKTLILGG ESCPAALAEY WAPKLRLILA YGPTEGCVVC IFSDASGHEC APGEIGRPVT
CEAWIVKPED PNVLCEVGEA GELLIRGPNV ARGYLNDQTK TDRQFVHELA WIPKTNDARH
RGYRTGDIAR YMDDGRLCWV GRVDNQVKIR GQRLELEEVE KCLHECSNKL GMGLKHVVVD
AVTLSGMASK QLIAFLCLNT EEPVGYLAWD VEGSSVATPQ TTPDEQARCL SIISKLETTM
RSILPAYAIP SIWIPLREVP FTVSRKRDRN RLRTIVAPLS AKQLSVFLHP TTSNISNGSK
ASLSENETVL QGLWATVFGI DRSSVEVNDN FFSIGGDSVL AIRLAASARS NGLNLSLQII
FQNPILADMA RITESISGQD EEESMIPPFT LLDSDWDIQK VRQEAASQCG VDYISVEDIY
PCSPMQEGLM ALSSKDAGTY VLRFVFHMPT NIDLDKLHAA WETVSKRTPV LRTRFVDYNA
DLLQAVIREP IDWKATEQDL DTFQDDDNDS DQVLGKRMSR HTVLRQSGSK EPILVWTIHH
ALVDGWAESN ITAAVEEVYR GNDAPSSSTP MFNRFIKYLG EQDQNSGKAF WRKQLAGAPT
ARFPPLPHPT YVPKIKRSNK IAELTAEQGA ELDHRIRFAK GGSATAATVI QAAWFILVGL
YSNSSDVVTG VTLNGRTAQL PGIDQIAGPT ISTVPFRAKI DRDQSVDEYL KSIQDKVLSI
LPFAQFGLQN IRRLSEDAVS ACKFRSLLLV QAANRPAGSS KLILERSFAF PVMDFAIVME
CELSKDGIDM RATFDHNILS QAQVQRMFLQ MEAILQRIMS RTSSSRVADL QTISDTDLSQ
VIQWNREGCI QEDISPFVKE LIQQYAIHHP RLSSTSDTQS GDYPGKPVQA FDTLAWIVHP
EEVNILVPPG AIGELVLEIT NPRGPALQYL GTLTSFPTWA QSLQRTSSVE FIKTGDLVVY
DTDGTLRLVG QKVDHVQIGG RPVDLSEVEC RLQEVLPSTI AAAIAFVRSK DGNESKLVGY
LGFGRDAQED VPNSLLVNDD EDLEKLNNVV DDAETKLRSI IPSYMRPSEY FPFRMIPLTP
SGKVDRGKLE QLRPSSTPIQ PLSIGHKSAR SKMRVPLTKM ERRMAKLWKT LLDVDHVGGD
DNFFQLGGGS VLAMRLVSMA RREGLSMTVS GIFNTPTLRE IASTVRQKTD TVDIAPFALL
PGLDITELLH QAALQCQVKD NEIEDIYPCS FFQLHYVTGY PEACSDPRVD PWHWQSQGAY
SLPPSLNLDR FQAVWNMAVQ RHPVLRTRLV HTPTGIFQAV IKTSKPAKWN RGDDLTEYLL
RDQVNYMTFG QDLLRLGIVQ SQASDERFFV FTAQHVIYDA FMRSMLFKEV EAAYFDDFPH
NPLPKMNKFI KYITETDKDS ATRFWTTYLE GANTKPLLNP VEKPGLLSVS EKRMVTKSAK
PLDQSLAEVS LPTIIEVASA LAIARTVGCS DVVFYSDRSG RNLPVEGIQD LIGPTTLFLP
VRVNIDPKQE IHDLLRESQR VKTSMIPHEH LGFLELREM
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