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Database: UniProt
Entry: A0A1X1QZ48_MYCFA
LinkDB: A0A1X1QZ48_MYCFA
Original site: A0A1X1QZ48_MYCFA 
ID   A0A1X1QZ48_MYCFA        Unreviewed;      1010 AA.
AC   A0A1X1QZ48;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN   ORFNames=AWC04_19035 {ECO:0000313|EMBL:ORU96678.1};
OS   Mycolicibacterium fallax (Mycobacterium fallax).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1793 {ECO:0000313|EMBL:ORU96678.1, ECO:0000313|Proteomes:UP000193484};
RN   [1] {ECO:0000313|EMBL:ORU96678.1, ECO:0000313|Proteomes:UP000193484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44179 {ECO:0000313|EMBL:ORU96678.1,
RC   ECO:0000313|Proteomes:UP000193484};
RA   Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA   Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA   Olivier J., Enrico T., Nicola S.;
RT   "The new phylogeny of the genus Mycobacterium.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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:ORU96678.1}.
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DR   EMBL; LQOJ01000073; ORU96678.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X1QZ48; -.
DR   STRING; 1793.AWC04_19035; -.
DR   Proteomes; UP000193484; Unassembled WGS sequence.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR   GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
DR   CDD; cd05274; KR_FAS_SDR_x; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   NCBIfam; NF037940; PKS_MbtD; 1.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
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   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193484};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          921..996
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1010 AA;  103217 MW;  7BBBE0B2002518A4 CRC64;
     MVSIPTLPDG RIPVLLSAHA EDLLAADAAA IAGYLGAHRG AATVAEVAAA LLGTRRIRRH
     RAVIRARDHR ELREALAAAA AGTEHPRVAR SARTAAPRVA FVFPGQGGQH PGMGAASDAL
     PGYRAAVDRC CEAFAAAGHP TPRRYLMGTD PQHYTEIEVQ GAQFSHAVAL AEAWRAGGVR
     ADLVVGHSLG EIAAAHVAGA LTLADAVGVV AARAGVVDRL PGRYAVAALG MTAAEAMALI
     AETPGWLELS VINADGAVAV SGDRAAVTAA VATARGRGRL GREITVNFPV HTSVLEPLGD
     WVRANLPAGE FAEAAVEVIG ASTGDVVAAG TAFGDYWYAN LRNTVRFDRA VATAIRRGAE
     VFVEISSHPA LLHAVAAQAG DGALLVGTGR RDTEPADEFS ANLARVAVAD PGHRWYPAPG
     PRRLPGLPNA PMRADRLWAQ RRPLPPVPAL TITAERWLPA PAEPAPAQGP RRIAVLELGV
     GAAVAQQADA QPAAAQPALA ERLAAALGSH PGAVAAEPTD ADTLVLLAPR HPEPDPEHAV
     GVLEHLVAGG LLDYPAAIGP ACRNIWLVTA GAEQVTGADP LLPLPAALAA IHRSLGLEHP
     ELNFAHLDLP EQPPAPAAVL GALLGAPGEV ALRVDGAGQT RCYRRELGAF DGPALHAPAL
     PTDTGLLDEV VITGGSGAVA RGFTEQLAER GARRIVLLSR RPADPDWCAA LTARYGTDIR
     PVSADLTDPD ALRAAAAAHA GTGATLVVHA AGAATFGPAA DLDDTAFAHT LAAKTTGLAE
     LTRCWPLARD ARVLLCSSMS AVCGGHGHAA YAAANRLLDV AAARLRAAGI GCVSVRWGLW
     QTPAGGIVDA AETARIQRSG LRPMAPAAAV DAGLCDYRVD PLILVADPDR LRIFLGCAPE
     PAPAPAPEPA AAPTPGPAAG TDPAALVRAE LAAVCSLPGP GAVDLGAALF DLGVDSLLAL
     ELRKRLTRGC GHTVPLARLL GGITGADLVG DLRAAASRGA NGTESDTPRD
//
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