ID   A0A168DTA6_CORDF        Unreviewed;      1559 AA.
AC   A0A168DTA6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Transferase family protein {ECO:0000313|EMBL:OAA72981.1};
GN   ORFNames=LEL_08765 {ECO:0000313|EMBL:OAA72981.1};
OS   Akanthomyces lecanii RCEF 1005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC   Cordyceps confragosa.
OX   NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA72981.1, ECO:0000313|Proteomes:UP000076881};
RN   [1] {ECO:0000313|EMBL:OAA72981.1, ECO:0000313|Proteomes:UP000076881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA72981.1,
RC   ECO:0000313|Proteomes:UP000076881};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
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:OAA72981.1}.
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DR   EMBL; AZHF01000007; OAA72981.1; -; Genomic_DNA.
DR   STRING; 1081108.A0A168DTA6; -.
DR   OrthoDB; 1591446at2759; -.
DR   Proteomes; UP000076881; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
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; 1.
DR   InterPro; IPR036736; ACP-like_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; IPR007817; Isocyanide_synthase_DIT1.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   PANTHER; PTHR37285; SPORE WALL MATURATION PROTEIN DIT1; 1.
DR   PANTHER; PTHR37285:SF5; SPORE WALL MATURATION PROTEIN DIT1; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF05141; DIT1_PvcA; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF02458; Transferase; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 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:UP000076881};
KW   Transferase {ECO:0000313|EMBL:OAA72981.1}.
FT   DOMAIN          954..1032
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          315..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          348..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..329
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        349..371
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1559 AA;  173352 MW;  C03DF3CAF7EB2856 CRC64;
     MAAQKSVSQS ILDIITEFSL NKFDDSAQRI VAGTPSFLAV IDAFVAAQQE VQTCLPSFPF
     KSANKQYKVL GSLPDKAEEL ALARLNNMCR RIREVYSPGA RVTIISDGMT YNDLLSISDS
     ETWQYGEALR RMAQAKGFSH ISFARIRDLV DCELPEKLRE ITYVANCTNM RRILLNEHGR
     DDLDIDQEIV DNPDTKLTYL GYCRFLESDL KHIFPPDKDR TNRAYKRDVK YLAKQMLRRG
     YAFAGAVKKA FPTHLRLSIH ESLGEHKVSI SLLNTQTGFT TPWHCSVAQL ADGEWISAPM
     GEFQKDDRLE LVHEDGRPSH FKEKPRGVDS PPSISETWAA FMPAAKKFSP SSAGSSSPTT
     SLLSSREGQV TPGASPRVLG LGISGCTTPA GSYTSENELS AAKDGRSPDY GRRLLPQIID
     ELAASHPEQS LFSLSSMVKN VLEFRDVSAR QFAKAVDKTA WWLQEKVGKP AAIQPIGYIG
     PHDLRHILLT YACVKVGYAA LFLSPKNSTQ GALAVLETLN CHIWAKAGDA PLVPLVQDVL
     KERPMTILDL PSLDTLLDSA NTPAYPYTKT FAEASADPFC FLHTSGSTGI PKPIPWSNGL
     IGTMDAIRLL PRVDGDHDLL PWTTNWCAHD RIYSSFPMSH GAGIIMNILL PALFNLHCIM
     GPVNILPNIT LVEALAEQAR IDIWSMVPSL TDEVGETPDV LAKLAPSKFI CASGGPVSPV
     SAGKANKVIR VLNLTGTTEG LFIGNLVPPR EDWFWFAFHP YSGFEFKQLD EDTYEHWIHR
     DEQHASLFQG IYHTFPEQQS INFKDLYMQH PTKPYLWAFK GRNDDLVVLS NGYKISPLQT
     EAFIATHPDI NGCLVIGTGK PQAALLIELK DPNGKTEEIL DSIWDTVQEA NAQMRHKNQL
     LRDFIAFAEA DKPFVRTDKG TVKRPATLKV YEDYIERFYS SRNSDIPVFD VDLSSLESIQ
     HDVRELFASY LAEVREVPLD ANLFELGFDS LAVFAAIKTL RIVTGLADRL SARQLYANPT
     LGGFSSILLE LSKEIKEQAG NGQMSELQRL MAKHQARQSF KLNAMDYVNP NHYMGLVFYF
     PLADGVDFQQ VFDNLSKGLD RTMDLIPALG GKMVPCSEHE IGHTKGDLCV TIPPLHMASS
     VHNRLIYKDC SDTLPTFAEL RGKDFVPSLF RDEIILQQDT FPNLPTDIVI AQANFVKGGC
     ILAVDMNHCC LDGMGVMIAL KAWAENCRYL QGDATATCSW LDADSFNHSL PEIIHHQEGW
     TKSADEVDPG TWGFLPFQPA EDAPPSKYIP TAGDLPPPPK YKLHSVWPLP RAERCMNTTV
     VEISAENIRK LKKQVLADPA TKGSSASVSD IVQAFFWRSA IRARRHVAKA TGNDMSDEQD
     VSILESPTDG RAHFSSLLPE TYMGSMLIMS RSVLSAEELC APKTSLGRIS QVLRDTAARI
     TPSLVHDAFN ILQSLPDHTR FSTANMGLDH MHAMISNLIL FQMSEINFGN KLFGNNGSPE
     TMRPQLVRAH GRFRFLIISP MKKDGAVELV LGTFPEELDF FKQDEEFSQY AKVVDVSPW
//