ID A0A2C6ACA8_9HYPO Unreviewed; 1908 AA.
AC A0A2C6ACA8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN ORFNames=CDD83_4996 {ECO:0000313|EMBL:PHH89906.1};
OS Cordyceps sp. RAO-2017.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=2004951 {ECO:0000313|EMBL:PHH89906.1, ECO:0000313|Proteomes:UP000221130};
RN [1] {ECO:0000313|Proteomes:UP000221130}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1346 {ECO:0000313|Proteomes:UP000221130};
RA de Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PHH89906.1, ECO:0000313|Proteomes:UP000221130}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1346 {ECO:0000313|EMBL:PHH89906.1,
RC ECO:0000313|Proteomes:UP000221130};
RA De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT behavioral manipulation genes and a possible major role for enterotoxins.";
RL Submitted (OCT-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:PHH89906.1}.
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DR EMBL; NJEV01000251; PHH89906.1; -; Genomic_DNA.
DR STRING; 2004951.A0A2C6ACA8; -.
DR OrthoDB; 2301216at2759; -.
DR Proteomes; UP000221130; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd19534; E_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; 2.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 2.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 3.
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; PTHR45398; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR PANTHER; PTHR45398:SF1; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF00668; Condensation; 3.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 5.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Ligase {ECO:0000256|ARBA:ARBA00022598}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000221130};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1819..1838
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 778..854
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1908 AA; 208594 MW; FAA1465E89BBF621 CRC64;
MASAIKQKLE WRPSSAADHD CAPALPPLPQ QPAADEAVEL EFPWPQERPT DSRMLLLVRA
AWAVVVGRET NSKDVVFGGA EPERSTTTSA TGTTNGETAV QETEPAAVHV QWTSDQKVTD
YLEAVQQLFE PTQCPGESPS SRQYQTCTLR TTCMLPVRTQ QQRSAADDLG VPRTHAVVLE
AQLGQEIKVT ARFDQRLMQA RTGLSLLQRL ACVAGQLAAA APEQAVKEME TATGRDIQQV
WAWNGEVPPA VDRCVHELVE EQARARPDAV AVCAWDGELT YGELDRLAAR VAGDLVGRGV
GPDSLVPLCF EKSKWTTVAM LAVLKAGGGF VLLDASLPEQ RLRNIVDQAD ARLLLSSPSR
LALSSRLAPV VLLISSDSFA HPGNQPDRPL PLPSPSSVMY LVFTSGSTGN PKGVIVTHRN
FSTAVLYQAP DLGLSAESRV FDFASYAFDA SVSDTFLVLA TGGCLCVPSD QDRAGNISLS
IASLKANVVD VPPSVAPFLI PQELPDVQTL IFSGEALHTR HFHRWWDRAR IINVYGPAEC
SPISLVNGEA SSPEAAVRIG RGSGAVTWVV DPDNYDCLLP VGCVGELLLE GPLLGRGYLH
EPAKTAAAFI HDPAWLLRGA PGRPGRHGRL YRTGDLVRYN EDDGSLSFVG RRDEQVKIRG
QRVELGEVEH RVHECLPQAR QVVAEVVAPE GSSAALAAFL EMPDERSAAR LLPADADVED
RLGKLLPSYM MPSIFMALPE MPKTASGKID RRRLREMGAS LSAQQLADTR TTSGTKRAPV
SKTEQQMQAI WAQVLNIDQA TVGLDDSFLR LGGDSITAMQ VASAARSRHI HVSVADILGK
KTISKLVDGL EPSSVGEPVS RALVSHETLG GRSMQLSPIQ NLYVQLQPDP TKCCFDQNFF
LSVNGRITRD SLSAALETIV RRHTVFCARF TRNQEGMWEQ RITPDASASF RLFVDESGAD
KTAHAIAQCR DSLNLEDGPL FAALLFDDPA ATQRLFLTMP HSIVDLVSWR VLLRELEALL
TSGTLTMPPP LGFQSWTALQ AEYAAEKLDP AVTAPTEVRP PLLEYWGMDV KENLEGGAVF
KRSTLDVATS SAILNGCNDA LSTRPLELMI AALLHAFGLV FSDRPLPPIF SEGHGREPWD
DSIDISATVG WFTTLWPVQI SSGKNASLID TIRRTKDCVR ALPRKGWSWF TSRFADAEKA
ARFASGFPVE ILFNYQGLYQ QLERSDAIFE QIDLPHGSAP ASSSAVQRFA FFEIDARVER
GRIVTSVAYH KEMGHQQRIA EWVEKYEETL VQMSKELPEM LPSWTLMEFP AVFSSYEDIE
EFQNVWLDRL GILRLEDVED IFPCSPMQEA ILVSQAKDSN NYRPWSLYEI KVRGEGARLD
MARLQQAWQA VVRRHGLMRA IFVDGLPGSD GTMHVVLRDP SPSISVLEEA GEAMVSRLRN
MDDTGASYPK LGLQHHVTIC QLDAATAYMR LDINHTISDG FSQDLVLRDL QAAYHGSLGP
AGTYRDFVAC LAEQPKDAGI EFWSGRLAGV EPCLFPALGG DDIDRAAAEA VSVKVPNLDA
GKIRAFCTRW TLTAATLTQT AWALVLSKYT GATMPCFGNL YSGRDVPVHK AETISGPLMG
MAPCRVLIDR SKSVLDTLTK VQEDFLGSMA FQHVPLAAIH RALGLGTSAL FNSTLSFQRP
DDEGRVGADS VVVRNVYECD PTEYDVTISA FDRGCLSQAV SEIISDPTRS LGELDLLGPS
DLEQIWGWNK TLPEPAEQCV HEMVKAKAQA HPDAPAICAW DGNLTYGELD LLASRLARRL
VDSGVEPGMM LALCFDKSMW TTVAILGVMM AGGSFVLLDP SLPEQRLQFA CQKARANLIL
SSTANQTLSL RLCQKVVAFD SDFFDQLDKT ASSIDDLPSV DLDSIIYL
//
