ID A0A1V4D8F9_9ACTN Unreviewed; 1272 AA.
AC A0A1V4D8F9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN ORFNames=VT50_0209595 {ECO:0000313|EMBL:OPF81648.1};
OS Streptomyces antioxidans.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1507734 {ECO:0000313|EMBL:OPF81648.1, ECO:0000313|Proteomes:UP000033615};
RN [1] {ECO:0000313|EMBL:OPF81648.1, ECO:0000313|Proteomes:UP000033615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC164 {ECO:0000313|Proteomes:UP000033615};
RA Lee L.-H., Ser H.-L.;
RT "Genome sequence of Streptomyces antioxidans MUSC 164.";
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:OPF81648.1}.
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DR EMBL; LAKD02000019; OPF81648.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4D8F9; -.
DR Proteomes; UP000033615; Unassembled WGS sequence.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR CDD; cd08956; KR_3_FAS_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 Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
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; INACTIVE PHENOLPHTHIOCEROL SYNTHESIS POLYKETIDE SYNTHASE TYPE I PKS1-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM01294; PKS_PP_betabranch; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1116..1194
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1197..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1272 AA; 133650 MW; 1BAAF5A133BAA1D0 CRC64;
MLDRTVFTQA GLFALEVALF RLVESFGVRT DFVVGHSIGE VVAAYVAGVW SLEDACTLVA
ARGRLMEELP AGGAMASVEV SALEMGRVLE GLRAESGLCG VVEVAAVNGP DQVVVSGEEA
AVAEVVEYWR GVGRKVKGLR VGYGFHSALM EPMLDGFRRV LEGLSFAAPD MAVVSNVTGR
PVEVGEVCSP EYWVRHVRQA VLFGPGVEWL AGEGQVTRFV ELGPDGVLAA MAHNCLAHHI
DADSEDGSGA EPEVIASLRR DQPEVQAVLT CLARQFTTGA SIDWTPVLGE SDSNAPGAHP
GLPTYAFQRQ RYWLDAPHHT ADVTDLGLET VEHPLLGAAV PLAEGGRVFA GRVSLRTHPW
LVDHQVLKTV LVPGTVLVEM VVRAADRVGC GRLDELALEA PLILTEEGGV QLQVVVEEPD
ESGFRPVAVY SRPEDQESAG GAVWVRHATG SLVAGESAVG GGVVLEQWPP VGAEPVVADL
DAFYERFSGR GFDYGPAFRG LEAVWRRGEE VFAQVRLPRE RVGEAERFGV HPALLDAAVH
AMALIASDED EGGDEEAARI PFAWSGVRLH ASGASVVRVR LTRAGSDAVA LEVADADGQP
VVSIESLALR PVSAEQLQAA RTSRYDSLFQ LDWQPLESPR ASVAGGSWAL VGPDVGLGEA
VVREGGSCVR YADVSALIGA LDEGEAVPET VVLSCPTSGG EDVAAGVRES LATVLSVVQR
WLGEERLFGS RLVVVTCGAV ATEADEDVAG LVQAPVWGLL RSVQTENPGR FLLLDHDPDH
DLECGSEISP AAADAAVRVL VAGEESQLAV RGGTVLVPRL SRVTKSAPSQ ASAPLVSGGT
VLVTGASGVL AGVVARHLVA EHGVEHLLLA SRRGPDAPGA AELVAELEVA GASVTVVACD
VADRDAVREL LAGVPAEVPL RGVVHTAGVV DDGVVEGLSD ERVWRVLAPK VDAAWHLHEL
TADMGLEAFV LYSSVAATLG AGGQGSYAAA NAFLDALAQH RHAHGLPALC LAWGLWAQAS
GITQNLSQTD IARMARGGTT GLTTEEGLAL FDTAQSVGRP HVMPVRMDLA SHQAHPEVPV
PSMLRNLIRT PLRKAATGQS GAKQWRDRLL GASPEEREGL LLDLVRVSTA TVLGHRDSGD
IDLEGEFLEM GLDSLTAVEL RNQLGGATGL RLSTTMVFDH PTPADLAVHL ADELNSLAAT
SPGSPNLPSS PSSPSSPNTP GVANPNTAGT HAVLAEIEKL RETLSLASLV DEDRSLALGR
LEDVLNQFAK QD
//