ID A0A2T3AIH9_9PEZI Unreviewed; 4037 AA.
AC A0A2T3AIH9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN ORFNames=BD289DRAFT_48521 {ECO:0000313|EMBL:PSR99255.1};
OS Coniella lustricola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Schizoparmaceae; Coniella.
OX NCBI_TaxID=2025994 {ECO:0000313|EMBL:PSR99255.1, ECO:0000313|Proteomes:UP000241462};
RN [1] {ECO:0000313|EMBL:PSR99255.1, ECO:0000313|Proteomes:UP000241462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B22-T-1 {ECO:0000313|EMBL:PSR99255.1,
RC ECO:0000313|Proteomes:UP000241462};
RA Raudabaugh D.B., Iturriaga T., Carver A., Mondo S., Pangilinan J.,
RA Lipzen A., He G., Amirebrahimi M., Grigoriev I.V., Miller A.N.;
RT "Coniella lustricola, a new species from submerged detritus.";
RL Mycol. Prog. 17:191-203(2018).
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DR EMBL; KZ678385; PSR99255.1; -; Genomic_DNA.
DR STRING; 2025994.A0A2T3AIH9; -.
DR InParanoid; A0A2T3AIH9; -.
DR Proteomes; UP000241462; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 3.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
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; 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; 1.
DR Pfam; PF00668; Condensation; 3.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 6.
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:UP000241462}.
FT DOMAIN 2131..2209
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1861..1905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2103..2126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2250..2271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2724..2755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2828..2853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3007..3241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3359..3414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3450..3479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3511..3548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3570..3606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3621..3886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1862..1888
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2106..2126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3007..3021
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3037..3064
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3093..3109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3130..3148
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3151..3181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3190..3210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3359..3381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3392..3414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3531..3548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3570..3584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3585..3606
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3627..3691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3698..3712
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3713..3740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3778..3801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3812..3886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 4037 AA; 432784 MW; 8326B1E5F1D0220A CRC64;
MAEDPTQAER FSCPKIDITS STSPNLGIHT DNSQPSDRPH TLQERILSSV ANSLSIPPER
LRETFASHAA DDDDEDQDEG DHHPLASLNP NDAPRSRLDR LTIQTKVLAG SKTIADMETK
IEPPSARSMA AEVVDMASYE SESDATTQGE EPEQQAAQQA EESDDSSDDD STDDGFDMRS
ASIMIAPERI HRASRMNSIQ VRNQDFDKHS LDNAPPMPTN SYETPGEVER FLGSEKGVSK
VVIIKPRAGL FEEKLVACLT LASIQPSSPD SAKVDLVSPA QSFFAGTQIA TIRHNLQESK
FVDKNAIPQV WIPLDKMPMV PDTDNIDRRK LRTWVQNANS EIYERVMGIV TDQTIQHPET
EMEREIQRLV GRVLHVPQEQ IGINFTFASL GGDEAAAMAL VTTARVESIF LESHEILHHN
NTLAHLATLA TQRGGLAHKW TAQRESSEVD GDTSPSSAYF DLSPMQKLYF TTAMGGNLAL
RDAGDARYRF NSSLLFRVAK GYTAHDISAA TDAVVGHHKM LRARFVNVQG DWTQYIMPKV
EGSYSFMHYV VSTNQQVEAV VQTVQASINV ENGPLFAVAH LETTDGHQMI YVAAHHLVVD
VASWRLIIRD MDELLQHGSL ASPRAMPFQK WTELQKMDAQ MPSGGLPFDL CPGDLDYWGM
MEAPNTYADA NEASFSLSSE LTAILETTCN QVLRTESVDI YIAALLLSFA QTFVDRRVPD
VWNQELGRNL WNVDIDISET VGWFTSLCPL NQQLNASSDL VDVLRRLKDT RRAIPHRGAH
YFASKFYSDL STGNDAAEAE EGSIAAGQGG DSGPVQPRSP GCLQIATRDW PIEILFSYAG
NVQNIAKENG VLEQIALPGR TIDSPISDIG PAVGRIALFE VNTTIDQGSA RIKFLYNRHS
RNVSLIQTWI SNYEHLLLEA IGRLRFAEPE WTLADIPQLW ATGATYEGLA TLNKTINAEL
GLGGVNDIDA VLPVSPVQQS ILISQAKSLQ FPAGCGTKHG DDHGERQYAP PYPHSSNNAN
MNAYHIHVMY ELVSPDGATV DLSRLVAAWV QVVAHHAALR TVFIESIADQ GLFNAVVLKR
WAPNMLFLDA TPAEDPSVTL NNLPPLTAYP ADKSVPRHRL TVCQSALKTV IKLDVSAALC
DMMSVNGMIA DLRRAYTTGR AVSLSGSDVA AFSYPGYLDI MRNLDRARSI AWWQQTLASV
TQPCIFPRLD LYYGGEAEDP NRPRRYDSVH SEVGDVTLQK VTDFCRAYKT TTGTVLRLAW
ALVLRSVTGS SDVCFGYRAP GRSATLEGMR SAVGCFANTI PVVLDLSQFK PLAILLKQTE
DGYNAALPHQ HITMAEIQHA LLQDRKGSGW NAQLFNTCFA YTEEPADLLG RLHSHSTSTS
STAAATSTTA LELRNVMNHE TSDYDLTVNT RFSNATGRLV VDIGSAILSE TQAQNMTNTF
ARAVMAMIQC ASPSAHIGSL DLFSDRDYSQ IVEWTHPLDK QNEQRQQRSL LHELVFAQSI
NRPESKAVCA HDGDLTYAQL EVLSHRLAHV LLSAGVVPRS KAKAAVPVLL DKSKWVPVAL
LAVLKAGAAF VPVDADEMGF VAKIAEHLGP AGKVAVACVA AADALAMSSD QQVPLFDRVV
RLDDALMQRL EHETVAAGTL LPPSKPEDVA CVFFTPTSSR SIRGISFTHA SLSTCFVGQG
PVCGINHSAR VLQLSSFNVD VALSEVFTTL VHGGVMCIPP SRDRYSDYTG CVTRFGANWS
YMTPLLSRKL NTELLPTLQT VCFRTRGLDA DTYRPWHGKK RVIMAYGAPD VCPLGISFLE
LHGPHHLRAI GRPIAGSAWI VSGEDHRNLM PVGAVGEMVI EGPTLGKTFR RSSLHVLVNE
DDCATGNNNS NNNNNKDLPD TPTSPGGSHG KTPFVRGHHH NQKSISTIAT EDTGQGKKRY
YKTGHSVRYI EGGLMEYVSS KRDDLEINGR VVNLSELEQY IRRALGQGID VMVEALAFKG
DRAAVPFLAV FLELGDFDDG TRGAGAGGPP SSAPSCAPSS AVALDLTSLN DEVKQRVLVA
KRLVTKALSG VVPEAIVPKT FIPVRHLPTT HSLKVNRRRL QKIIKGLSRD QLFDLARPGH
ASQLDCGGNN HGNGNNSDNP SETTTATTTI LPAGSLEASI RAIWAQVLGR VDPDSISLED
GFIKAGGDEI AAAEVVVRCR KAQLGGVSIS DLMRDLPLGE MCRVNMPLDA LPGTYQSGYP
LVAPSREPSQ AGAMVLDTAL DDAIASIQRQ QQEHTEYFDQ DQAGQTQHGL SVATPPLLPP
TPQIIDKAFI DEKLAPKLLL EPEVIRDVAE ATSTQVRHIE TALLTQGRVK PSAGSNSHGP
GLADMTYFVF HFTAASSTSS VSARRIEEVC HILTSIHPIL RTAFVAHVEG QSRKLYQVVL
RNHQADFKHI ARVQSWRLGA TLDKEVRKDR EMLHTRCDLF ARPITRFLFL DAGKTSALVL
RLSRAQYDDV SIAHLVKDLR KLYDGSQNPP RRPGFADFVR EAALAHVGGE AERYWRGLLE
GAVPTQVVHH THPPKPTTAV RTLRECVSVH TIAMGSLGIS FDTVLKAAWG MVLATIGGVP
DVLFGELVEG CHSRMQQHLG PSSVNRGGVL GPTTALLPVR IRFADSATSP LHLLKCVADQ
RAAGIPYENL GMLNIVEKCT PWPYWTRLST VVQHRTEAEL LMDGKAKSFR LGATLCKISV
LESEMMDVPD FLVRSLLKSK GGAGAGGAST GGGPATDHGV VDGGGESNGG GTARFHHQGD
EELEISVSFC EQRVPATLAQ EVLHKVCGFV GLLTGVSIMQ SIVPTAAQYS ALAKQIPFAN
ALYGMSGNNS SSSNNSNKNN SSSSNNASSG PAGVTFNNPF GGGAVRATFA QLEAKMSLDQ
VTTIRATIED AWRSTLDPRT LGVPEEHVTS AAFYDLWGSL IPAAQLADYI SEEVPHRLVG
DELSRNLFNN NLDGFAVTMD EIVDHPTMLD QFQLVVRKAF GGEGRDRGGS VLRMRSASAG
AAAAAAAGHS TTNSMRRSHN TILGGSHGGG GGGGGSTAGS IRSNSPTMSL HSVMTSTRNG
ASSILHGPSK LGGGGGGGGG YGRGHTRTRS DSTEHTMGSS NTHGSGGSVH TDSPALGGGA
PVFPAHPAVK PPIHHHHHHH HHHHDHHHQY GQGNSNSQAR NRKGSDASNA TYHSANSSGI
SAPAGAGPGG FTNMTNTTAT PPTTVGSPDL SELPGSPGAT LAPQPLSTTA AAASAAAAEN
GHDGTGTGAG LGAGLGLGAG SLKRANSVVR VRESELGPES PILGNANMAT SPPVVQAGFG
VASAVGSVSS ATGRKKSNFG FGSSLRRIAS NALRPGLQSH GHGQSASLNS LKSSGGGSVL
GGISGGNSSN NSNNLSLRPP MSSGSDRAGG LFSPKDTTNT TTMTNKNPNN GPVSPWVRVP
SMAPQLPPFS PFTPVTTDDA FSLVNEDGTT VSGSASFDTG LSRDLSSQGR ATSRGTSPDL
ILQCTTPGAG AGMNTPTMGV GDDFVVVGGG GGGGGAERGR RAELGIGEGY GGSDNNNNNK
KKKQTRISGT LVMDENGQLT RAVSFESFTE SVTGGVGSGA EVSSQSQDDD DDDDDNDDEN
EDEEDTLRAE DAHKLLAKAV HLAGNGGSSP SKASRTRSPD LYHQYQQQQQ REQGAKRRTA
SSTLTSTTTT TTTTATAIKR AQLQDLPSPS PVTETFYMED DEGSEESDGD VSENDQQQQQ
QQQATYYSND AHSSSHVSYD SEDGGAAAAV KYQPQPPPAD TSVKSDKTNH AGGEGGKAVQ
PSQSQSQQTQ AQTQQSPRYS VFPRASVHGS PPPARPTSST AGQNKQQQQQ QQQQQQQGTT
QTTAALAAAT SSFSSSSSSS SSSSPSNQPQ SQPAQQKPTT TKQQIPDPQD YASLEAAEMD
DIVSPLTPVE RAMLYKQQGL MQMHGGGVGV GGGQNRFHVG ASRMGSNSGV SIGSGGGGIG
SSNVSPLTPG SFFAQQGLQA QQMDSQQGQQ PGQWYYQQGQ QFQGDEGRNQ QQQQQYQQYQ
HYQHYQHYSS IGGFHAI
//
