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Database: UniProt
Entry: A0A023BPR4_9FLAO
LinkDB: A0A023BPR4_9FLAO
Original site: A0A023BPR4_9FLAO 
ID   A0A023BPR4_9FLAO        Unreviewed;      3516 AA.
AC   A0A023BPR4;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Carrier domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ATO12_04990 {ECO:0000313|EMBL:EZH71976.1};
OS   Aquimarina atlantica.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Aquimarina.
OX   NCBI_TaxID=1317122 {ECO:0000313|EMBL:EZH71976.1, ECO:0000313|Proteomes:UP000023541};
RN   [1] {ECO:0000313|EMBL:EZH71976.1, ECO:0000313|Proteomes:UP000023541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22II-S11-z7 {ECO:0000313|EMBL:EZH71976.1,
RC   ECO:0000313|Proteomes:UP000023541};
RA   Lai Q.;
RT   "Aquimarina sp. 22II-S11-z7 Genome Sequencing.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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:EZH71976.1}.
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DR   EMBL; AQRA01000010; EZH71976.1; -; Genomic_DNA.
DR   RefSeq; WP_034246254.1; NZ_AQRA01000010.1.
DR   STRING; 1317122.ATO12_04990; -.
DR   eggNOG; COG2898; Bacteria.
DR   eggNOG; COG3321; Bacteria.
DR   OrthoDB; 1230081at2; -.
DR   Proteomes; UP000023541; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd08953; KR_2_SDR_x; 1.
DR   CDD; cd00833; PKS; 2.
DR   Gene3D; 1.10.1240.100; -; 2.
DR   Gene3D; 3.40.47.10; -; 2.
DR   Gene3D; 1.10.1200.10; ACP-like; 2.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 2.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR   InterPro; IPR049490; C883_1060-like_KR_N.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR024320; LPG_synthase_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR049551; PKS_DH_C.
DR   InterPro; IPR049552; PKS_DH_N.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF21394; Beta-ketacyl_N; 1.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 2.
DR   Pfam; PF00109; ketoacyl-synt; 2.
DR   Pfam; PF02801; Ketoacyl-synt_C; 2.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF09924; LPG_synthase_C; 1.
DR   Pfam; PF21089; PKS_DH_N; 2.
DR   Pfam; PF00550; PP-binding; 2.
DR   Pfam; PF14765; PS-DH; 2.
DR   SMART; SM00826; PKS_DH; 2.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 2.
DR   SMART; SM00823; PKS_PP; 2.
DR   SMART; SM01294; PKS_PP_betabranch; 1.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00606; KS3_1; 2.
DR   PROSITE; PS52004; KS3_2; 2.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000023541};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          9..82
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1000..1425
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2423..2497
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          2568..3005
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   REGION          490..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          958..980
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2500..2533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        490..506
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2519..2533
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3516 AA;  396164 MW;  067731AAD425B10E CRC64;
     MIDKEILLES TESYLKSLIS QFSQVPIGDN CVSTPFQELG IDSFRILQII KKLEEEFGTL
     PKTLLFENFN IGDLSYYFVD KHEGILREKF KQEKEGNDRA VYSNEESSNS TEEITEIFDN
     RYDVNKEETP VLILEKEANK HPELLKLVEK LFNQYKNEGS ASRGTRNIAP NLFIGAEKKG
     YFNYSRYKDI ILVYSYTGAK DYLSVITEEI YQYCINNNFE LNLFTVDQVE SIRGVLFTAT
     PFGVLSRVNI KDFTLQGSKM RRLRYQVSKF ERAGKCRIEE YQNGSDKKVD KNITQIIDEW
     CAPRTMVNPL IHIVKEEILS GNLSAEHRLF LTYLDDVLQN VILISKLSSE ENGYLMDLEF
     YPKSMPLGGL EYAIVEIIKT LKAEEYTTLS LGGTYGCKLN SSSNADPELD KTLDYLRGQN
     IFNDEGNLQF KNKFRPEHNT VFLSRPVGSN PDNVTDIIMM IADPMKMQTS DEENHTFTKL
     DKQTVALESK TARQNTSNSN GEFKQVKENP QVEKHKVVIE GEERSIMLSD YGYNPLNIPG
     DQVTFDLKTD SWAQLELPVI QNQLSFLYTQ LQQPVDLVES LKNIFPFSYF TLTTAGRTAE
     RAFCKSWPKK GKVLQNLLFP TMIFNQIENG FTPIELPHPG VYKLDAEDQY KGNLNWEALK
     KQVEEDPESI AFVFIEMNDN AAGGAPVSLQ HLKQVKTFLS EYAIPLVFDT TRIVENALFI
     LEHENEFIGK NVWDVVREMV SYADAIIASL AKNFCVDKGG LIGTNDVELY NKIQNFIQEE
     SIGLDVIDKK VIGLSFHNRN KIEAWVRNRL QSVQTIWRVL KQQGIPVVQP ALGHCILIDV
     KQIPEFELFE YPVASFVSWL YLNTGIRAGA HNVGMQKDTE INNLVRLAIP VGLKQEKIEE
     IANRLIKAFQ KKTNIPEILP KDNQSETFGN IHTNFNLKKY HNTSGKVVSK TLNSETSSID
     NDNNFSITES TGKSTQTDSD IKVKETGANQ NIQNDKPYQT GDIAIVGIAG RYPKAKNMNE
     FWNNLVQGKD CVEDIPDVRF GQRLHNKFSE KYRGGFIDDI DKFDSLFFNI SPREAEYLDP
     QERLFLEVAW EAIEDAGYYP ETLVDDNASR NIGVYVGAVW TLYQVIGTEE KLQGNFVSPS
     SHLWGIANRV SYAFNLSGPS LPIDTACSSS LSALYLACEA IYKGECSGAI VGGVNLDAHQ
     SKIDINKSGG ALSADGVCRT FGKGANGYVA GEGVGAVYIK PLDKAIKDGD HVYGVIKGIA
     VNHGGKTSGF MVPSPKSQAQ VVTTALESGK IDARSIGYVE AHGTGTELGD PIEISGLTAA
     FQEYNVDKQE CSIGSVKTNI GHLEAAAGIV GLHKVLLQMK YKKLVPSLHS SELNPFIDFK
     NSPFYVEQTV KEWKPKTIEG VQYPLRAGIS SFGAGGANAH VIIEEYVTPI EEEKTPSSKF
     KEYIFPLSAR NENQLRETAI RLSTYLQDDL SGEKLLTCKD IAHTLQIGRK SFDHRLVIIA
     KTKQELVQKL TLFIDGKQDN AMLTGEVKNS QNITRLLNRK EKEEFIKFLS QSGDLSKLAQ
     LWSVGFLADW QGIQALEAGA KISLPTYPFA DKRHWISDTS KSSNLSLHST TALHPLIDSN
     ESTFERQVFK KTFHDKDFFI YDHLVSEIPT LPGVAYLDFA RKAGELATGR KVQIIKNILW
     LSPLTVVDSV PKEVCIELKP NGGLVHFEVF SEEENNTKQI YSQGKLIYAT HEELTAEPEY
     IDLEEIRTRC VKVTDGKEAY PLFKSLGLDL GPSFQVLQDI FKNDDEILGE LLIPEIRNND
     FNDYLLHPSL VDGSFQAGMA AQLGEQTGEM FVPYSIGEVE VLQPLKPKCF SYVKKVDEPG
     SKVSKVNVFI VDEDGMILVK IRESIGVPLV SVHEKPDQTK EEEEYSKLYY SHEWKKSLLE
     QEKVLSNESG PILLFSPDEK LQKVYKDRYK KNEDIILIEP GDKFKKLGSH KYKINPQNPA
     DFKKLFEALN KDIIKNICFA WPIGDELKDD DEYEEGFIQK SFDNGIYSFL MLCQSLIEQK
     LDNVQLLYLY LGQIGTSQPH HEAINGFAKT LQMEHPKLYC KILEIQQSKK SYDKILDIVL
     TELHSDNSNE MTIRYQEEER YVRKVKEFSL LQDQDSDRTD SFGLKEKGVY IITGGAGGLG
     LIFAEYLAAQ CKARLVLTGR SKLSGERQTK LDRLSEVGAE VMYIPADVSI AKDVENLVKK
     AKSKFGKING IIHSAGVLRD SYVRSKTREE MEAVFAPKVY GTLYLDRITK DEDLDFFVTF
     SSLAAVGGNA GQCDYSFANH FMDSFAEKRK LLQEKGERSG VTLSLNWSLW ADGGMKLDEQ
     TEIFFKKNLG IKPLSIKTGL EAFEKGLHTR KAQFVVLEGV QEKIERAWGI KEKETPEAVA
     TDSKTSTDSE VQVDQQADKE LFIVVRDALS KIVMEMLKLD PEDISYDKIL LDLGFDSIGL
     TTYANRINEL YELDITPVLF FEYPSIKEIA TFLSREHKNE VQKTHEVSGG TSTSDIKKEA
     SQPAKRKEEY SDAEKGILSI NKGWNASALD QQSQSPGEAL STESRFIDQP IAIVGMSGVM
     PGSENLEEFW ENLENEKNLI TVIPEDRWNW EDYDGDPFRE KNKTNSKWGG FMSDVDKFDP
     SFFGISPREA EMMDPQQRIF LETVWKAIED SGHKVSDLSG TKTGLFVGVA TRDYADSLVD
     NQIPLDGYTA SGNSHSVLVN RVSFLLNLRG PSAPLDTACS SSLIAVHRAI ESIHTGSSDM
     AIVGGVQLML TPAAYISFGM AGMLSGDGKC KTFDKSANGY VRGEGSGAIF LKPLDKAEAD
     RDHIYAVIKA TTENHGGKVT MLTAPNPVAQ TDLLVEAYQK AHIDPSTVGY IECHGTGTSL
     GDPIEIQALN KTFSELYKKH NKAPAKTPHC GLSSVKTNIG HLETAAGIAG VLKVLLSLKH
     KKIPATLHFE ELNPYINLKD SPLYIVDKTQ NWEVIKDDQD NTLPRRAGVS SFGFGGANSH
     IVLEEYIQEE DHSQIQLDEP HIIVLSAKTE DRLKAYTQLL YNHVEKHDIN LTNLAFTLQV
     GRDEMDERLG LVVNSIEELK EKLSDYLSQK ENIEDIFYDR VKQNSAAVID STEKNDFSET
     QIDKYINDKN YSRLTEAWVM GIHIDWAQLY KQVKPRRISL PTYPFARERY WFNLVDSEKL
     KSAGEFEKLH PLLHYNSSTL SQQCYTSTFS GKEFFIKDHK IQQQNVMPFT ACLEMAYVAV
     KNAMPDLNES TTLELRNTFC VNLLTIKDNK EVNISLVENN DKGVDYEIYS IEGEKEIIHC
     EGEVVILANQ NSTNIDIVQL KTHFTTQAIN PEELYQVLKQ MDMSYGPSFK GIKNFYKGED
     QILAQLSLPE TITDDYKNYA LHPSLIESSL QLAIGLLTDL DSKLNQPILP FEIGSVKLFS
     PCQKELYAWV RYSKGSKQED DIVNVDIDLT DKSGEVCVKM KSLAFDSTLY KQTKKNTYKD
     FEMLINAIHN GDTREQEYAE TENSETSFNQ LLKDLY
//
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