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Database: UniProt
Entry: A0A251XC74_9GAMM
LinkDB: A0A251XC74_9GAMM
Original site: A0A251XC74_9GAMM 
ID   A0A251XC74_9GAMM        Unreviewed;      1012 AA.
AC   A0A251XC74;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN   ORFNames=TPSD3_04020 {ECO:0000313|EMBL:OUD15690.1};
OS   Thioflexithrix psekupsensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Thioflexithrix.
OX   NCBI_TaxID=1570016 {ECO:0000313|EMBL:OUD15690.1, ECO:0000313|Proteomes:UP000194798};
RN   [1] {ECO:0000313|EMBL:OUD15690.1, ECO:0000313|Proteomes:UP000194798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D3 {ECO:0000313|EMBL:OUD15690.1};
RA   Fomenkov A., Vincze T., Grabovich M., Anton B.P., Dubinina G., Orlova M.,
RA   Belousova E., Roberts R.J.;
RT   "Thioflexothrix psekupsii D3 genome sequencing and assembly.";
RL   Submitted (DEC-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:OUD15690.1}.
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DR   EMBL; MSLT01000006; OUD15690.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A251XC74; -.
DR   OrthoDB; 9757559at2; -.
DR   Proteomes; UP000194798; Unassembled WGS sequence.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd08953; KR_2_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; IPR049490; C883_1060-like_KR_N.
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   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF21394; Beta-ketacyl_N; 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:UP000194798};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          919..994
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1012 AA;  111956 MW;  D1F71F6F5DD320A1 CRC64;
     MILCRDHNEA VHALQTQNPQ RVFTQHVTQN TSVAFLFPGM GAEYLGMANT LYQQEPLFRE
     AVEDCLVHLR PLGINLTDLI SSHNPSDGLQ GIPYRHAPVA LFVVGYALAK FWQRCGVEPA
     AMLGYSGGEY TAACLNYVCS LEAMLTIMVI SGQTMETLSE GALLAVAAPE QQVKEQLNGD
     SLSIAAINGP LQCVVAGTVE AIEALSTRLQ QANIPCHRVP GQRAFHSSLA EPLAARLHSA
     FQNVSLHAPQ TAWLSGVTGQ WITPQEATDP RYYAEKITLK PVRFADSVTP LLSEPDLLLL
     EVGPGQVLTP LVLQHPKWSR EQRVIASQLD PRYGQSEHAA LLTALAKLWL SGVDIDWQGF
     FALESRRRLP LPTYPFQTQR HWIDPKPLTP TSVTQQQTKK KTNISDWFYV PTWQRIALSP
     APLPPADNER WLIIGKANVA ISLYKQLKSR GCAVIWGQFG TEFSKMSAEC YQIGLDDPQS
     YFKLCQNMAE QGFIPTHIVH TGLVNSPKGA GLAYGFYSVL YLMQALTQQW IGEAARLHVL
     SNTMQSVLGT ESLVIEKSAV LGLLKVIPQE FSHLICSSLD LDGEGADVDC IAQILDECRS
     SHSRRTVALR AGHRWEQHVT AVSLPVAQNS EGLKQDGVYL ITGGLGRIGL LLAEFLAERV
     HAKCVLLSRR TLPDSSQWTD YLSKNKPDDP NYQVITRLQN IRSLGGDYEL MTGDVADTQA
     LQQAISQAKQ RFKRLDGVFH AAGLVGDESI RLIAQTDRDY CEKHFQGKLY GILALSQVLR
     DEPIDFVMLF SSLSSILGGL GFGAYAAGNC VLDAVAQQCD TKNHWLSVNW DGWAFETQEH
     DSGKVGASLE ALAMQCHEGL KALQTALLYK NHRQLIVSTG DLNSRISQWV ETDTSDAGAI
     SFDTTAKNNR PHLMTDYHAP RDDIEANMAR LWQGLLGIDP IGIYDNFFEL GGNSLLMTQL
     ITHIRKSFHI ELSLTDLFNA PFVADMAEQI KTLRGEKPDR SLDNNDWEEG EL
//
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