ID A0A139I438_9PEZI Unreviewed; 3607 AA.
AC A0A139I438;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN ORFNames=AC579_8008 {ECO:0000313|EMBL:KXT09506.1};
OS Pseudocercospora musae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT09506.1, ECO:0000313|Proteomes:UP000073492};
RN [1] {ECO:0000313|EMBL:KXT09506.1, ECO:0000313|Proteomes:UP000073492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT09506.1,
RC ECO:0000313|Proteomes:UP000073492};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the NRP synthetase family.
CC {ECO:0000256|ARBA:ARBA00029454}.
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:KXT09506.1}.
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DR EMBL; LFZO01000336; KXT09506.1; -; Genomic_DNA.
DR STRING; 113226.A0A139I438; -.
DR Proteomes; UP000073492; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0009403; P:toxin biosynthetic process; IEA:UniProt.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd19532; C_PKS-NRPS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
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; IPR013120; Far_NAD-bd.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF20; HYBRID PKS-NRPS SYNTHETASE APDA; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000073492};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2026..2103
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 3174..3251
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 2109..2187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2110..2125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2128..2155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2157..2176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3607 AA; 393345 MW; 0280976DB96AF689 CRC64;
MPWPSGASPR RASLNSFGFG GTNCHAIIEQ YVPSSASPAG TAGVPPNRQD SFAGPLLLSA
STGASLAASI NGLADMLEAQ CEDESSNSDS LEDLAFFTQG RRTTFPQRIS FSGGRSKKSL
IDALRSSTAG MAPENVGVRA PTRLRWHNPG ILGIFTGQGA QWATMGRDLA HKCFVFRKSL
QHCEAALASL PDGPSWSLME ELAKEQSESR VSEAELAQPL CTAIQIALVD TLAAAGISFR
GVVGHSSGEI AATYAAGLLS AEDAMRVAFY RGLHAHLAQG ERGQHGAMMA VGLGIDDAEA
FCMGFDGRLS VAASNSPTST TLSGDQDAVL SAKDLLDERK TFARLLKVDT AYHSAHMLPC
AAPYLASLKA CDIQVRPQNN ECIWISSVHG HAELLDDPAE LGVLADEYWV ANMCQPVLFS
DAVECSLWRA GPFDLAIELG AHPALKGPAT QTITTALGPN ALLPYVATLQ RGQNDVSAFS
ASLGSLWTTL GHWVDLDGWR RGYLGPDCTA SATVIKSMPS YSWSHDQIYW KESRLSSRYR
LADRRPHELL GRRVADDSDH EMRWRNVLKV SELPWTRGHV FQKAILFPTV GYVALAVEAA
AEIAGLDRIK LIEVHDLIIP RALVLEDNHA GVEIVFSVRR RQPASNDALT IDTDFACHSS
VQGGTLEKNV SGRLIIELFS SPDMKDDDSD ICVLPELRPS RSGTTSIEGE AYYQALLKTT
GLDYTGLFRG MKHVRRTLGF SSARASWPAE DVGDQYIAHP GLLDVALQGL LAAMVNPTRI
PVQGSFLPSA MSRMVINPHA RSLSDDGTEV VFETDCVLTK NTARSCEGDI HVFGPSAQCI
LQVEGFRMDN WKQLSAKEDR PVFSYLDYQP DLFHGNGSNL PELYLDEDEQ KLIEAINRSS
LYYLRTYFSS VSDAQVASWT WDRQAFYNSV KLVLQHTSNG KHPNLQKSWL EDTADLMDSY
KQTPAFRDQI DMRAVHVAGE HLAKVMAGEE RPLEVYLREN VWAKLYSHGR YQIRLNRTIA
DLVRTFSHRY PRAKYCEVGG GSGGTTQSVL AALGDAVGQY TFTDVSAGFF EKTRERLAHT
DAEAAGRVVY KVFDVERDPV EQGFEAESQD VVIAANVLHA TTDLTKAVQN VRRLLKPGGY
LFMLEVTGEF LEGLLLMGPL EGWWLGNREG MASQPGLSLQ GWDDLFRSTG FTGVDKHQSD
VPDLDTHAIS VVVTQATDSR VEILREPLEF LDDVPLSDQV LIIGGQSLAM AKTVRSISQY
LARFVGRVQV VQSIDKIDPD IHTAGSTAVI ALCDLERPFF ADPVTETRLQ KLQALFAQAT
DMLWVTSGHL DDHDPHAAMM VGLCRTVVIE LEQLNLQFLN MATKSSRPVD ARPIVEAFVR
LQLGASDDFR LQPVLWSTEP ELTLTPEGEM LITRLKPDLE RNDRLNSAGR HIVKAVDSGD
VAKHRYTAVS RDGYIKFEEA EPWLCDVSGR QQELAGNTAI RTTISVNLPW SSSTVLATGL
DKENRPVLVL TNAHSSIITS ASASSLALDS TTPCNAQQLI ACALSILAQQ VLTTIPRASS
QRPKVVIHGA SSDLAQVMAK LAGDQLQLVF TQSTASVKSS NAHIVPLHPR ASTHNLQRSL
PANVDYVVGI VKDDPVTTKL LSILPGIKFD CDALLLEGKL LPLAELGPVV SQTLADMIDV
VEQKTLISAH RLPGLPSASL EYPAVVDWNI PPASSMQVTI NPIRGQGLFN PNKTYFLVGL
VSSLGRSICR WMVENGARHI ALASRSAKID PQWLEEVSQL GAKVVVYRMD VSEKSSVQKT
VATIRAEMPP IAGVANAALV LRDRLFLDMQ ASDMNEVLGP KVNGSLYLHE EFSEPTLEFF
ILFSTLSCII GNAGQSNYDA ASLFQVMLTK HRRQQGLASS VIDVGAVADV GYVAERGQAM
FDKLARTMKL PLSEIDVHQI FAEAVAASPV RDGETVSSTT GDIITGMGPY VYDSNTPGEA
HPQWYKNILA SHYVREEQVS STLAGGADAD PLSVTARLEE TTSEDTVAAV LTQALAARVE
TMLQMSPGSF KIDIPLLDVG IDSLLAVELR TWFLKEVHVD VPVLKLLSGE SGESICAFAA
SQYLAERSKA KTEAGPRDFA TPETDSEHDG IASMSSSVVD QSLSPSGTSD TGDSAVEMRM
SDGEAEHKEE EVDDTSSPPG LKSTAPMTHA QTRMWIADQM AADHTRNNNI LIYDVKGYVH
IARLRRAVAT VVAHHEGLHT CFFQDGTDSP WQGLLETPME CFKHIPASSE SREAVQTTQN
ELRARKWRLQ HGQALEVVLI SHTSDEHTLL LGYHHIAMDG SAWRTFFRDL HMAYQGAALS
APGKSPISLA IEEATHDTVS DGLSTFWSKQ FSAPPELFPL LPFASVKARP GLERTSNHTV
LVELEGTIAD RINAVSRSLG VTSVNFYLAA VQGLLSRLAE TDDICIGVTD SGRDAETAES
MGFFVNMLPV RLRTSNSGRF GELVKEVNTT YREARAHANV PFDAILDKVG IRRDPTCTPL
FQVGFDVRPG QSAAIPLGNC QLNIVDSIDS TMPYDITFLV VPMPVSGPSF VQVITRTDLY
SREATELLAQ MYITFLSNAM RQSVVDFPLG KLQIYPGAMV ERALEIGKPG RKAFDDWPST
LTARFDRILK SHSAVTAIKD VDGSLSYAEL AEDVMSLAAR ILPYRGRRIV VICEPQRAWA
ISMLAIWRVG ATFVPLDATL PLARLVTMLR ASEADTVLYH AATGELTSQV VSESESTVQV
LLLEDTPACG TGHVVDNLED PSTASTILCT SGTTGVPKAI LLTSRGLLNY VANQHDLLGV
KPGEIILQQS NLGFDLAIAQ CLFAFCHGCT LIIAPQTSRG DPVALTNLML KENVSLTFAT
PTEYLMWLCY SGDVPSRLNR WRLAISGGEK VPLTLRKEFE NLLHRPHFAD CYGPAETSVS
STIPHDTDRL AEDALTIGAT SIGRPLANTG IFVIDSKGHV CPPGIPGEIG ITGDGLALGY
VDPIATAKAF VDSSKYAIDS GEGIMLHEGT MYKTGDRGVW RSDGTLGFLG RLSSDTVVKI
RGIRVDLSDV EHAILSQGSH LISDAVVVLQ QDNDDVFLVA HVSPVVNNRH DLEAPLEDFM
RQLPLPRHMK PTRVVLHTRL PVNANGKADR GALARVPLPP RKASAEHYDD ATAGMATLTQ
VELHMLWARV LGRSDIPRRA DVDFLAMGGS SLHLVKLQAA IRTDLLVNLS IRDMFMHSTL
GAMAELIENR ISDLPAPDRI DWDQETRLPE DLALALSSQQ ITDQPPARDA AEVLLTGADS
FLGGKILRAL LQDPAIRRVH CIAVASVPAD VDHRRVVVHE SSSSLRQQNL GLSEDAVASL
MDSVDRIIMA GSYGHCLNNY FSLRQTNVVS TKLLAKWAAR RRVPLHYISS SRVTLLHKDS
QAALPPISVK DHHPPVDASE GYTASKWASE VFLEHLAQAA GGAFPITIHR PCALIGAEAP
SEDALNAILK FSAEMGAIPR VSQINVHGFF DFAPIEKVAA DIVTDVLAKP QPQHLLFRHY
SGRVKVPPNE FKAYMERFYN KEFVELELEE WLTRALEVGI EPLITVYLRA TFGGGGNHRI
VFPYMGA
//
