ID D4DGK9_TRIVH Unreviewed; 2154 AA.
AC D4DGK9;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN ORFNames=TRV_06313 {ECO:0000313|EMBL:EFE39039.1};
OS Trichophyton verrucosum (strain HKI 0517).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663202 {ECO:0000313|EMBL:EFE39039.1, ECO:0000313|Proteomes:UP000008383};
RN [1] {ECO:0000313|Proteomes:UP000008383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKI 0517 {ECO:0000313|Proteomes:UP000008383};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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:EFE39039.1}.
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DR EMBL; ACYE01000359; EFE39039.1; -; Genomic_DNA.
DR RefSeq; XP_003019684.1; XM_003019638.1.
DR GeneID; 9583572; -.
DR KEGG; tve:TRV_06313; -.
DR HOGENOM; CLU_000022_60_2_1; -.
DR OrthoDB; 1744764at2759; -.
DR Proteomes; UP000008383; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR CDD; cd05918; A_NRPS_SidN3_like; 2.
DR CDD; cd19542; CT_NRPS-like; 2.
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; 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; 2.
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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 499..575
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1589..1665
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2154 AA; 239195 MW; 3B2464B5689F5EBC CRC64;
MSQLHISQLW KFNSGVSEEP WMECFHAVVE RHARENPLSQ AIDAWDGRFT YAELNNLSIL
LAKYLQSQGV GPGSVVPISF ERSAWAIVAM LSVSKAGGAF VSIPPYLPSG RREAMVQMIS
PSILLTTSDF CHLWATGPKC IPIEGSRINC LPTSELPLIT RSKPEDTFYI IFTSGSTGAP
KGCMVSHSSF LNGALRKAPE WKFGPKRRVL QMLSHTFDMS LLEICTSLGS GACVCVPRTE
DIEDSLANAI NKYNVSLAVM TPSLARQLEP EAVPKLQVLC LGGESFPKDL VTLWSERINL
FQFYGPSECS INSSTRAITH KNTDPLNIGV PNNAACWVVS PEDYNKLVPI GATGGAFGLW
CYCRPRLNGQ RLELGEVEYH LTLEEGVGHA MAMVPRTGRC KDNLMGIISL KSSPPVDSND
EISTLQGALV DQSIQSIRKR LQNSLPRYMV PTIWACILRM PMSASGKIDR VRVRRWVEEM
SESTFREITG GIQQPGDRNP LSKMEQFVQN IWSSVLDLSP QDVGRHQSFI QLGGNSILAQ
EVVAKCRKEG IGLTMTDILT CNGIAGAASL TTALGNNESQ TRLLSSTSTP VWRKLREKYD
LSRLGVSHIE DIEDVYPCTP MQIGMFLGQI RKPGSYHLRF FYKPIVKGGK LPELGRIESA
WHQVVSHHTS LRTVFVDDLG VGAEYHSVVL RNAPVDVCID EVPEKFSPSE AMETFTKSIK
RFAKRSTFHR ISLCVCGDKV TYLMIEVSHA LVDGAAMENL MRDFATAFDD GQLLYQPQPY
REFVKYVASQ NNEASARYWT TYLKDCPPCM IPVSKQMMFD DLPTRFLRKD FVYEKSSDFL
AKCKERQITV ASAVRVAWAL VLRAYIGSSD VCFTYVAAGR DVPVKDVNKM VGLCLSIQPC
RAQLCTGTTF VSLAERMQQE YIESMPYQHY PLTELKARLY PKGSEAMFNT AVSMEWTART
DPFYNTSIAF EEIREQDDPT EYDIVANVEI VDNIMKLGFL YWPSFSDIDV IHIANASKKA
LDCLLDSADK SVEAISLDGE HVFHAMKSSD QESLHHTETC VFDAIERQAM AQLNTQAVVS
WDGEYSYGQL TKYYTTYAKY LVEQGVNNGD IIVVCLDKSC WSVITILAIL KAGAVFVATN
PLHSQQRLES IVNHCQAKLI IVEPRYSSLF ETVDTPTVVV NKETVERALL STTLPTIRDS
DIATIVYTSG TTGLPKGIII DHGSLCTSVL QGHGKRYGFD EETRALQFAA FTFDACLQEI
ITVLSHGGCV CVPSEDARLS DLGGCITQMR VNLALLTPTV ARLIRSQDVP CLKRMILCGE
PMSRQDLEAW AGTVTLYNGY GPAEATICVS ISGPLDVSND PANIGYAVDG TRLWITEAAD
YNRLAPAGCI GELVIESRQV SRGYLHDVEK TNAMFINPAW LPGCRVYKTG DLAKRNPDGS
LTYCGRKDTQ VKLRGQRVEL GEVEYHVCEC WTNASGVVAE VIYPTGEDKA TLAAFVCTSD
AQNNALGDLD APEEPKTGLS PVWVSKEFIE QLEDRLPCYM VPSIFFTIPS VPLTPNKKTD
RQHLRDIGSN FTSEQLARVS DHQNNSKRMP LEARERKLQQ LWSFVLNIDR SQISLDDSFF
RLGGDSVSAM RLVTTARKSG INLTVADVFR HPHIDEQARI ASSSSNNILK TLIGKPFAHI
QRKDLERVVS LVGLGPYANI ASDIEDILPA TDLQSFYASR IAEASRDALN YFYLRFDNTP
DVTRLRHACQ SIVDQFPILR TIFIPTQGRT YQVVIRRLQV PLEIHNSVKN LSKASDLFCL
QDLENKIISG SLFLSFTLIR HAISGSQLII RMSHAQYDGM SWPLILRCFQ ESYAGVPRSP
TQSFSGFISY TIGKVSESRK YWTNLLQGSH VTQVSAKFTM ETPLQRVEKT HVEKTVELPI
PPKGITVASL VSSAWSLVLR QITGKRDVVY GFVVAGRNIG MPQIQEVVGP CMNTVPVRIC
FNSMRTTIDL QRHTMNQYFA MGDADSLGFQ DIVENCTQWP SGTKLDTLLQ YHDIDETPVV
TLSGGPDSEP CSAQLDWFRK PYAAPTNIEV SARPNGKTLG ITVSSDGSLL STESATAILT
MFERSIRILS NGRAIPLDSI NLLAVAARRN QPKIPDLCPP AYLTFQLLSL MLGS
//
