ID A0A0D1WJS9_ANEMI Unreviewed; 1254 AA.
AC A0A0D1WJS9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN ORFNames=AF333_13150 {ECO:0000313|EMBL:KON98523.1};
OS Aneurinibacillus migulanus (Bacillus migulanus).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Aneurinibacillus group; Aneurinibacillus.
OX NCBI_TaxID=47500 {ECO:0000313|EMBL:KON98523.1, ECO:0000313|Proteomes:UP000037269};
RN [1] {ECO:0000313|EMBL:KON98523.1, ECO:0000313|Proteomes:UP000037269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2895 {ECO:0000313|EMBL:KON98523.1,
RC ECO:0000313|Proteomes:UP000037269};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Fjat-14205 dsm 2895.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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:KON98523.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LGUG01000004; KON98523.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1WJS9; -.
DR STRING; 47500.AF333_13150; -.
DR PATRIC; fig|47500.8.peg.1385; -.
DR Proteomes; UP000037269; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd05235; SDR_e1; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR010080; Thioester_reductase-like_dom.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR44845:SF6; BETA-ALANINE-ACTIVATING ENZYME; 1.
DR PANTHER; PTHR44845; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR PIRSF; PIRSF001617; Alpha-AR; 3.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 3: Inferred from homology;
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000037269}.
FT DOMAIN 765..839
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1254 AA; 141403 MW; 23A3C03E2168E3B3 CRC64;
MERYWFDRLI EPLPVVGIPS DFPRSSVRGF KKESVIVSMQ DLWAQKIENL CKDKGVLIEV
LMLSAYFVWL YRITHEEDIM VGVRLSSGEQ GEAALTLPIR ISLTGIESFE HLITEVKVRL
SEAMEHRLAF RAYEDNRIKE NGEDAVIAYP AIFVMGDAAY EELSAPIVWN VDMHTHYHIE
TTFNNKVFTR ASIHRFIEQY ENILEAVTLQ PSVRFREIDM LSKEECKLYR KLNDTREEFP
SDKTLSAMFV EAAEQFPSHI ALSSDKGQLT YEELNSKSNQ VARMLRTHGL KQGDFVALFM
ERSIETVVGL LGIMKAGGVY VPIDPEYPQS RIEYMIEDSR AAFIVTKAEF AGILDESARS
CPHGAQVLCL DDMQLAQYSN ENVAAYPGAT DPAYMIYTSG STGRPKGTVI VHRSAVNLLV
YLRKPYECTP DDVFLQFASY SFDASIAETF SALLWGARLH LLSNMERVAI EEFANVAERV
KATGALALPT AFFKQIAAYL EDNSIHKLRT VKRIIVAGEA LTGETVRLWQ RRFGLNINIF
NAYGPTECTV GTTIYLVEKE VPPEQVYIPI GKPYDNYETY IIDPNGKLCP IHVPGELYIG
GAGLAKEYLN KPEKTAEAFV PHLFSDAPGA RLYKSGDIVR LLADGNIEYV GRKDNQVKIR
GHRIEMDEIE DVFAKQQDVE HVAVVAKTTE DGNKRLVAYY STGSTYPLDE SEIRKFLAQS
LPAYMIPEQF IYLENMPVSP TGKIDRKLLI AREDKISLRR ESGEIPQSET EKRIAEAWEK
VLGIDEVGVT DDFFEIGGHS LKIISILVLL KPHFPSLKIQ DFFRYRTIAA LAEYVEQAVD
KEVKPVRSSS DGEREWKDLI EPPVIKGARV GQRKAMEYVL VTGGTGYLGA HIVHEVLQQT
EAIVYCLTRG SGKNSPEQRL VDTLHFYFPD MDLSVFGKRL IAVEGDLSES NLGLSPDMRY
ELADRIDTVI HCAADVRHFG DAEHFEKINV RGTSLLLDII RGKQGTHFHH ISTVSVPEDL
AASGQWEHFV QYGDFSYSTV LENEYSNSKL RAENVIRTAM KEGVSATIHR VGNLVGRAKT
GKFQRNIESN AFYRMMKAML LLGTAPAADW YVDLTPVDYA SQAIVNLAAQ PEMEGRTFHI
CNPEQIHYTD FINELHAIGY EIALLEPAEY RESLFRLNGV EEKAEALELA MAQLEGDGAH
DSEYRYICKN AQEILAREGI YCPKPDHDLL RALVTHAVEV GYFPRAKEHI VVGK
//