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Database: UniProt
Entry: A0A495JVC7_9ACTN
LinkDB: A0A495JVC7_9ACTN
Original site: A0A495JVC7_9ACTN 
ID   A0A495JVC7_9ACTN        Unreviewed;      1178 AA.
AC   A0A495JVC7;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Amino acid adenylation domain-containing protein {ECO:0000313|EMBL:RKR92252.1};
GN   ORFNames=BDK92_6690 {ECO:0000313|EMBL:RKR92252.1};
OS   Micromonospora pisi.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=589240 {ECO:0000313|EMBL:RKR92252.1, ECO:0000313|Proteomes:UP000277671};
RN   [1] {ECO:0000313|EMBL:RKR92252.1, ECO:0000313|Proteomes:UP000277671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45175 {ECO:0000313|EMBL:RKR92252.1,
RC   ECO:0000313|Proteomes:UP000277671};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (OCT-2018) 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:RKR92252.1}.
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DR   EMBL; RBKT01000001; RKR92252.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495JVC7; -.
DR   OrthoDB; 2472181at2; -.
DR   Proteomes; UP000277671; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR   CDD; cd12116; A_NRPS_Ta1_like; 1.
DR   CDD; cd19531; LCL_NRPS-like; 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; 3.30.559.10; Chloramphenicol acetyltransferase-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; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF00550; PP-binding; 1.
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; 2.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000277671}.
FT   DOMAIN          1060..1135
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          275..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..306
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1178 AA;  125850 MW;  DD546F86BDD1F519 CRC64;
     MPSTADPDAG TPTTAQPPDV RGSVVGLSPQ RQALLARRLA QRGLASVTEP LIARLPRTGP
     EQRFTCSSGQ QRMWLANQFD PADPSFHVSI SQRMRGDLDV GALRQALADL VTRHEILRTV
     YVGVDGTPHQ IVRPPAPVPM GEVDLRELPV VDREPRARSL ARRAFAVPFD LATGPVLRAV
     LYRLADDDRV LLMTSHHIAI DGWSIGNALR ELAALYRWRL TTPAGPSAAG PPPLPELTIQ
     YVDYAHWQHE SLADGELADG LDFWRRQLAA PRASAELPIA HRPEPDATSD STSTGGAGTG
     TGTGTGTGGK VGLMIGPELL DRLRTAAGAT RGTTPFVTLL TGFKALLARY LGQPDVTVGT
     LVAARTHVEL EPLIGYFANP VALRTRLDPE LTFAEAVSRV RRTVIDGFAY QSVPFDRVVQ
     ELAPRREAGR HPFFQAALIL HNFSAGTPED WPGLDVRWWN SELDDMLFDL TLVAVPQPDG
     GLEATFSYRT DVFDAADIGR LAEGFTELLA GIAADPGQRL GDLPLLTPAQ RQWLLVDRQG
     PVREPTPQTA TFPALWARSR DRHPDAVAVA AVDGELSYAE LDQRAELLAR RLRASGVGTE
     TPVGICLDRT SAMLVAMLGV WRAGGAYVPL DPAFPAGRLR LMLDDAGVRV LVTQGAVRER
     MPDLCASVPE LINLDRDEER GCPPDPVTGD PPDPDQLAYV IFTSGSTGRP KGVQVTHGAV
     GNLLVAFGES LALTPADRLL AVTTLSFDIS VLELLLPLVH GARVVVAGNA EVVDGAALQA
     RLRDSGATVL QGTPATWRML LAAGELPTTV RHRLCGGEAF SRELADRLGG GALWNVYGPT
     ETTVWSAAGL VEPAPARPVA IGPPITNTRI HLLDRRGQPV PVGVPGELHI GGAGLARGYL
     DRPGLTARKF VPDPFGSPPG GRLYATGDQA RYLPDGRIEF LGRGDQQVKI RGFRVELGEV
     EAVLREQTEV GDAAVAAWSD GSDGDARLVA YVVPADGATT DAARLWALLQ PRLALRLPGY
     LIPATLVPLD RLPLTPNGKL DRSGLPAPTW GATDATPYVP AGDPVEAAIV RIWEEVLDVR
     PVGVETDFFA LGGHSLLAER VLARLRAYFQ LAAPTRVLFE APTVAGLAAA LIRLEPVPGQ
     VTAVAEVRAE IETMSPEAVA RLLDGSGQDE VFGSGGVG
//
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