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Database: UniProt
Entry: A0A428TC93_9HYPO
LinkDB: A0A428TC93_9HYPO
Original site: A0A428TC93_9HYPO 
ID   A0A428TC93_9HYPO        Unreviewed;      1936 AA.
AC   A0A428TC93;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN   ORFNames=CEP52_009617 {ECO:0000313|EMBL:RSL99659.1};
OS   Fusarium oligoseptatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=2604345 {ECO:0000313|EMBL:RSL99659.1, ECO:0000313|Proteomes:UP000287144};
RN   [1] {ECO:0000313|EMBL:RSL99659.1, ECO:0000313|Proteomes:UP000287144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL62579 {ECO:0000313|EMBL:RSL99659.1,
RC   ECO:0000313|Proteomes:UP000287144};
RA   Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA   Kasson M.;
RT   "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL   Submitted (JUN-2017) 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:RSL99659.1}.
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DR   EMBL; NKCK01000102; RSL99659.1; -; Genomic_DNA.
DR   STRING; 1325735.A0A428TC93; -.
DR   Proteomes; UP000287144; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   CDD; cd05918; A_NRPS_SidN3_like; 1.
DR   CDD; cd19542; CT_NRPS-like; 1.
DR   CDD; cd19545; FUM14_C_NRPS-like; 1.
DR   Gene3D; 3.30.300.30; -; 1.
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; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   PANTHER; PTHR45527:SF16; NONRIBOSOMAL PEPTIDE SYNTHETASE ASQK; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00668; Condensation; 2.
DR   Pfam; PF00550; PP-binding; 2.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
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:UP000287144}.
FT   DOMAIN          757..832
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1408..1484
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          743..763
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1936 AA;  213884 MW;  1277B34F2CDF5CF3 CRC64;
     MHIIDGGGGG GSAISIDSRE KSRIFPGVPV IKTLPLGSTR DPATFQDELL LAWTLACSPK
     LEELPGSYDW GYILPDGSVQ RQSFRIDNST FEAERTTSQA LEGIKKHEAL SEAPCSPSSG
     AKLFFGQLPY SLKTDRDPKG TDEDSLYLEV SVTDQSLEIS GRHSTWSGSS DVDQEVSNFI
     YVLKNVLEHP DRRLGDLLGA TAKDLDQLWQ WNQEVPPLIE RCVHDMISDV ARDQPDTIAV
     QSWDGNLTYR ELDDLSTRLA RHLRSRGVDI GTRIPLCFEK SRWAIVGLLG VMKAGGTFSL
     TDPSQPEARL RTIVEQTGAE LVITSVAQSQ LGQRIVNDGQ VIAVSADFFD AISEVSDETL
     PEVPASSPMY VIFTSGSTGK PKGVVISHEN YTSGAIDRAR LVGYDSTSRC FDFPSYAFDV
     SIDCMLCTLF SGGRVCVPSD EARMNDLSGA IRESKANMVH MTPSVARVLD PDIIPALDVL
     GLGGEAVGAS DAAEWSKHVQ LVIAYGPSEC TVGCTINNTL HISTGIGKAV GGVSWIVDPD
     DHNRLTPVGS VGELIMEGPV VGIGYLGEPE KTAEVFIEDP TWLLAGHGDV PGRHGRLYKT
     GDLVRYDPKN PGAIEFVGRK DQQVKLRGQR VELAEVEHHI RECLPPRVKI AAEVIKPENG
     APTLVAFLVE PNQAQSDAES TLFTEPSEEL SAALSHIDSA LGAKVPRYMV PAAFITLQYM
     PSLVSGKTDR KKLREIGNSI PREKFGSLQS GDGQEDEPET EAEKKLQRAW NKVLGAEVKV
     YKQSNFFGVG GDSLRAMRLV AAAREEGLGL TVAEIFSNTT FSDMAEKAVE ITETSEEERE
     IAPFSLLDQD WDINEARTEA ATLCSIEEDL VEDVYPCTPL QEALMALSAK VKEAYVAQRV
     VELPDMDTAE RLVNAFDVAQ QDCSILRTRI VQASGRGLVQ VVVKGHLEWY SGTDLKEYLV
     RDRDEAMDLG KPLVRYAVIT NTETGTVNFV LSMHHALYDG WAMPLIVERI NKAYTGGSIS
     RPAEFKHFIK YLNGMDRSSS EVFWRERLDG ANGPQFPALP WAGYQTAADS LLEVYVPLEH
     PPVNSTIATV IRAAWALVVS QYINSGDVVF GETLTGRNAP IVGAEEIEGP MITTVPVRVQ
     VDYEAPVSEY LQDVQEGTVS QIPHEHYGLQ HIRRLSPDAL EACELRTGLV LHPSTAGDDV
     SGEDLPADRL VPAGDEEAAQ EALKFNTYAL MLVCSIDPKG FLIMASFDSK CVAKPLMERI
     LDQVKQTAQM LAEKSQTRLG ELAYLTEDNW SDIREMASAS VDDEALKQYP GLVSAYIVDT
     HDARRILPKG AMGELIIRST AELDYAAIEW PAWLNTLYGD ETANLEGTLY KTGKLAKFNA
     AGSIEFIDQT AKTNAASLTQ RRPAKRVSAT SRKQRKLRGL WSRVLGLSEE DIGLNDNFFL
     RGGDSIAAMK LVSEARLAGV KLTVVQIFQK RTLYDMANAM EEADVENHEV VEVPAFSLLE
     AENKDEFVEK IVRPQLANPE WKIANVLPTR FLQEVAVKGT IQIPRFSTRY ELMYFDSAVD
     RVKLMASCRE LVSRNEMLRT VFVEHEDQGY GVVIEDLEAE FVHYEIDSQV EPFAKQLCQL
     DVLTKMPLGS VFVKWFLVEG EGDKACLIFR ISHAQYDEIC LPLILKQLSA LYEDKPVQET
     VPFSSYVGHV VRENIPKAVD YWKELLEGSS MSILRPDVPV EKKNHFAIQK TVDISSRSKD
     VTVATLPTAA WALCLARRLS TRDVTFGEVV SGRNIDFPNA DLVMGPCWQY APVRVKFSPG
     WTVSDLLVHV QDQHIASSAH EGVGLNELVR LCTDWPQTTD WFDTVVHQDV DHVETLDFQT
     ASSRMETVYV HEEPLREWKI QAFPSGDTLT LEIVTVQSWS GYAEELLEDL AGVLSFLAKD
     PEARLFEDEG VQEVIE
//
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