ID   A0A2D3VM57_9PEZI        Unreviewed;      2066 AA.
AC   A0A2D3VM57;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN   ORFNames=RCC_08343 {ECO:0000313|EMBL:CZT22638.1};
OS   Ramularia collo-cygni.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Ramularia.
OX   NCBI_TaxID=112498 {ECO:0000313|EMBL:CZT22638.1, ECO:0000313|Proteomes:UP000225277};
RN   [1] {ECO:0000313|EMBL:CZT22638.1, ECO:0000313|Proteomes:UP000225277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=URUG2 {ECO:0000313|EMBL:CZT22638.1,
RC   ECO:0000313|Proteomes:UP000225277};
RA   Ploux O.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FJUY01000014; CZT22638.1; -; Genomic_DNA.
DR   STRING; 112498.A0A2D3VM57; -.
DR   OrthoDB; 2787863at2759; -.
DR   Proteomes; UP000225277; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   CDD; cd05918; A_NRPS_SidN3_like; 1.
DR   CDD; cd19542; CT_NRPS-like; 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; 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   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; 2.
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:UP000225277}.
FT   DOMAIN          607..683
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   UNSURE          723
FT                   /note="I or L"
FT                   /evidence="ECO:0000313|EMBL:CZT22638.1"
SQ   SEQUENCE   2066 AA;  227157 MW;  41E96777B61325A4 CRC64;
     MDEDAVQVRV AFDSRVITQQ RMEFIAENFV YAIAQLSDSD SANRQLTTLQ GGSSDVHQAW
     EWNDIVPEPT RECVHNVISR KAIQYPLSPA IDAWDGSFTY GELEDLTTKI ALHLHSRSLK
     GKVVSLLFEK SKWMPIAAVS VMKAGGVCLA LDAQQPPARL KGIVTQAESE LILCAESNIS
     LAQQIGGHVL VVGPDRQWPR GDSSTLPTVV PSDALYVNFT SGSTGISKGA ISTHEGFCSS
     RTHQQKTLGF SESSRVLDFS SYAFDASWAN CLHSLTSGGC LCIPAQEERD NDLAGCLKRY
     NINSVDLTPS VARIVGRESL SQLSSLILGG EPVVPEDANL AGPDTKIFNV YGPAECTITA
     TLAELRPNDI SIGRGAGVCT WVVNTDTDTL SKIGEVGELW LEGPLVGKGY LNDPQRTKES
     FIENPSWLVA GVTGTCGRPG RRGRHGILYR TGDLVRYRAD GSLIFVGRKD TQVKIRGQRV
     ELSEVEQHIL DALPVDISAT VVAELINPVD TRGGALVAFV TLKDAEITDM TEQSHNAAVE
     NAVAGVLASL AQVIPPYLIP AVIIPLQRLP LLSSKKIDRK ALRTLGASLY TQHRNTGSRA
     EECLDLQPSN DAETILQQVW MCVLNLSMDE VPINKSFARL GGDSITAMQA VSQGRLRNIS
     FTVTDVLEAS TIRKLAPRCK LVAPPQAFEL SQLGSAEEGT GDGNPFDLSP IQKMFFEAYP
     EGLNHWNQSF LLELERPVST TLLDNALKAV VARHGMLRCR FEKDTRTGQW IQRVMPKTDG
     DASLLQAHVV DSLEQVFKTS RSRQQSLNLQ HGPVFTSDLF QISSTGTQLL LLSAHHAIID
     LVSWRILWVD IEDFVDHGKL LSHPTASFQQ WCHHQIVVGS SLSPLSVLPY VFPEPPLNFW
     GISPSDNTYA GCEAHELSFD SNITSALFGA VNEALRTEPI EIMIAALMHS FLQIFPEREP
     AVVWLEGHGR ESLDETPIDV TSTVGWFTTL HPLVVPISLG STLVDTVRLA KDNRRRVPNK
     GQSYFSCRYH SESGREIFKG HGLPELVLNF SGQFQQLEAR GGLFTRPDSF GVENSDIGEI
     APTAKRTSMI EVNAAREENQ FLVTFYIHKD LKHRERLKEW ITSFSHTVES ATEELLRHAP
     SFTLADLPLL PLSYSGLDML LRQQLPRSGI LPSDVVDIYP CLPAQEGILL SKQKMAASYS
     TSTVWSCVPG QGGSSVISTS MLEEAWRTVA QRHTILQSVF VFNPEGEGFV QVLLRDPHVH
     IVTVDAINXT AVGRLEKLEG VKFTSREPEH AFFICQSSTG EVACRLDACH TLIDAASLSR
     LVEELTYEYE GTRLDPATPF RDVVSHVTSI PKDQRLSRWS KLLQNVKPCQ FPIQATKSHH
     GGTIERFSYI YLPQPAVEGV TAFCRLQNVT RFVFIQVAWA LXLAHFTGEK DVCFGYLSNG
     RDTPVAGIED VVGPLMSLLV GRVDLRGSVE EVLHNTSQAT ITHRSIQHTS LAEIQHHLGI
     SSQNLFNTTL SVRAADKLAK KGGITFHPQA GEDMHEFDVG LSVMIEHDAM EVVLEYRESC
     ISAQIAQEAA RVLAQAFEFL LTTTSDQDSN THLEIRDASD SFFRHVVGSE SPVARKFWSE
     QFAGIQVSHF PSTPLTPTVE AVDDTLELDF QDFTSEGQEF TASTVLRAAW ALLACRMTGS
     YEAVFGITVP SDTNTGTALP MRVVVDMQDS VAKFLRRIES QGDDIRQFGR IGYHWLKSLN
     DEAAVACDFR AVVEVLDDAV ELPPMHAGAI SIRCIMSTQR CTRLQLRFNS SIMAREQATR
     MLRQLKQITS RLLDTSLRDQ TLNSVDMTSL EDLQQIWRWN ATVPAAVNST MHELITLKAH
     EQPSAPCVCA WDGDLTYQQV DDLSTKLAIE LVVRGVTPGS VVLLLFEKSM WMPIAALAVM
     KSGAVAMATD ATSQSEQRLV AMVEKVQAAV CLSSLANVGL AGRLCGTVVI VGSELYKSPL
     YAPERLLPAV GAKDILFVQF TSGSTGVPKA VKITHGNMCS AVTHQGRALG YHKDARVLDF
     ASYSFDVFWS NLLNTLIIGR FPVPKA
//