ID A0A1T3NQJ1_9ACTN Unreviewed; 1655 AA.
AC A0A1T3NQJ1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN ORFNames=B4N89_33455 {ECO:0000313|EMBL:OPC79014.1};
OS Embleya scabrispora.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Embleya.
OX NCBI_TaxID=159449 {ECO:0000313|EMBL:OPC79014.1, ECO:0000313|Proteomes:UP000190037};
RN [1] {ECO:0000313|EMBL:OPC79014.1, ECO:0000313|Proteomes:UP000190037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NF3 {ECO:0000313|EMBL:OPC79014.1,
RC ECO:0000313|Proteomes:UP000190037};
RA Vazquez M., Ceapa C.D., Rodriguez Luna D., Sanchez Esquivel S.;
RT "Draft genome sequence of Streptomyces scabrisporus NF3, endophyte isolated
RT from Amphipterygium adstringens.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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:OPC79014.1}.
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DR EMBL; MWQN01000002; OPC79014.1; -; Genomic_DNA.
DR STRING; 159449.B4N89_33455; -.
DR OrthoDB; 2472181at2; -.
DR Proteomes; UP000190037; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR CDD; cd19531; LCL_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR029058; AB_hydrolase.
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; 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; 2.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF13193; AMP-binding_C; 2.
DR Pfam; PF00668; Condensation; 1.
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; 2.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000190037}.
FT DOMAIN 506..581
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1546..1621
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1530..1550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1655 AA; 176853 MW; 157AD31EA0842C15 CRC64;
MSSTAFPELD PAAPLAAVVD ARIVHMPASI AVIAGEHRLS YRELGEQADL VGARLAAAGV
TGGTLVGVCL PRTPHLVATL LAILRAGAAY VPLDPEYPRD RLEWVIGDSQ APVVVTDHAH
EHLLAGAATR LVHVDGPPPA DPTPARAATG PDDLAYVLYT SGSTGRPKGV RVTHRGVVAM
LRWAADTYRP DQVRGVLCST SVCFDISVYE LFFPLAVGGT VILVENVLAL ADAPARDEVT
LINTVPSAMA ALLRGPGLPA GVRTINLVGE ALSRRVADQV YACPQVEYLY NLYGPTEDTV
YSTWAVVDRT DRAEPLIGVP IPGTTAHVHA EDGEPAAAGE LGELYLAGDG LAQGYHGRPD
LTAERFVTVA GERRYRTGDL VRRRPDGALE YHGRVDQQVK LRGFRIELGE IEAVLTGHPG
VQAAAVVLRE DAAGPFLAAF VQPAAGTPAA GPADLRAHCL TRLPAYMLPD AVSLLPELPL
TLNGKIDRKA LPEATRSRFV AAEFVGPRTP TETRVVATFH DVLGVPRIGV HDPFLDAGGN
SLLAVGLLAR VEREFGIRIP LDTFFALPTP AAVAERVDRA EPGSAGPLVE PPYRDPRTPV
LVGTVQREFA THELVAPGSA LYNVPLRIRA IGALDPVELS RALGELVRRH EVLRTALMFR
AGAAVAEIRP PYPVEVPLLD LPDADPAQVE AALRPYARRP LDRAEGRLLR AVAVRTGPDR
YELLLVIHHI AMDGWSIGLL LNDLARAYQG VPLGEPALQY RDVAAWERRH ADAHEDEARR
WAGRLTDLSP EQYLPGDRTH ADPFDPSGAR FARRLDAGLV RAAEEWAAGE GASLYMAMLA
ALGILVNRYT GRTDQAVLTP FAVRPLPELE DVVGPLLNTV PLRFRVEGTD SFRELVHRLR
PVVLDALDHS ALPYLEQLRF AGVAGADTST PVSQLLLAVQ NHPGAAVELP GLTLEFLEEM
CNGGAKTDLS MFVEFPASGP LLSVEYRTGR YDEASIATIV DHLMAILAEG LAAPDRPITE
TIMLDPAEYA RVVEGANPAP TARPDVCLPD LIAAQIARTP DAIAVSAASG TLTYNELDAL
AARLARTLRY YGAERGTRVA VAMPRTHLLP AALLAVLRTG AAYLPIDTDQ PIARNRALLD
DAKVTLIVGE SAHAAGVPLL ADPGYDVVLV DGDEVRLAPA ATPDPGIEAE DPAYLIHTSG
STGRPKAVAV PHRAIVNFLL SMAREPGLTA ADTMAAVTTL TFDIAALELW LPLVVGARVE
IADRETSADG RRLADWLDRR EVTVCQATPA TWRMLLEAHW PGRPGLVALC GGEALTGDLA
GALLDRCARV WNMYGPTETT VWSTLLRADR AHAALRVVPI GTPIDNTRVY VLDSAGRPAP
VNAPGELCIA GAGVALGYLG NAETTAERFV HDPFGPPGAL MYRTGDIACR RRDGSLEFHG
RADHQVKLRG FRIELGEVEA GLTALPEVNA AVASVWDAPA GPTLVGYVVS ETPFTAAELT
AALAERLPRH LIPGVLIPLD ALPLTPAGKI DRKALPEPRP GGSGAPPEGD CEEILAEIWH
ELLGPARIGR DDRFLGLGGN SLQALRMAAM VEERFEITFP LRVVFEAPSL AAMARRIEDI
LMAEPEDPEE FDAGVDVVEH TGPTPYPAPT AGDVR
//
