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Database: UniProt
Entry: A0A1Q6Y915_9CHLR
LinkDB: A0A1Q6Y915_9CHLR
Original site: A0A1Q6Y915_9CHLR 
ID   A0A1Q6Y915_9CHLR        Unreviewed;       513 AA.
AC   A0A1Q6Y915;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN   ORFNames=AUH05_15970 {ECO:0000313|EMBL:OLB34339.1};
OS   Ktedonobacter sp. 13_2_20CM_53_11.
OC   Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC   Ktedonobacteraceae; Ktedonobacter.
OX   NCBI_TaxID=1805233 {ECO:0000313|EMBL:OLB34339.1, ECO:0000313|Proteomes:UP000185646};
RN   [1] {ECO:0000313|EMBL:OLB34339.1, ECO:0000313|Proteomes:UP000185646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(2016).
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:OLB34339.1}.
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DR   EMBL; MNDA01000455; OLB34339.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q6Y915; -.
DR   Proteomes; UP000185646; Unassembled WGS sequence.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   CDD; cd08955; KR_2_FAS_SDR_x; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036736; ACP-like_sf.
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   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   PROSITE; PS50075; CARRIER; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          439..513
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   513 AA;  57215 MW;  68489F3BBA72291D CRC64;
     MYSKNGEQAI GIVYLWGMLT TSVNESMRQP LRANQDLVSI GVLHLIQALT AAKKETSSRL
     WLVTSGVHTI EEQDRTTALS QAARWGLGRV IVYEHQNLHC TLIDLDTTPS EECLGTLFRE
     IWSDEEADEV ALRGDRRYVA RLTRHALLHG QGQAEALFRS DGTYLITGGL GGVGLRTAQW
     MVEQGARHLV LMGRRGGTEE AEATLQAMRE TGAAVRVLKG DVAREEQLAN ALVTIRREMP
     PLRGVFHCAV VLDDSTLLQL NRERFLGVMP PKVDGAWNLH RLTLDEPLDY FVLFSSAASL
     IGSPGQGNYA AASAFMDMLA YYRRQQGYPA LCINWGRWGE VGQAMKENRG KRLDFRGFAS
     MKPKEGLAIL RSLLHQSPPQ VGVMSFNLPK WSQFYPNLTR SSLFAHLLEE PGAQQENRAG
     GPLLTSEMLA ELDDELRQQT LMQYLSDQIA RVLGHTSLKL DAHQQLNRLG IDSLMSVELK
     NRIGSDLNVV IPVTAFLQDV TFEQLITQIL EQI
//
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