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Database: UniProt
Entry: A0A1V4D8F9_9ACTN
LinkDB: A0A1V4D8F9_9ACTN
Original site: A0A1V4D8F9_9ACTN 
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
//
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