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Database: UniProt
Entry: A0A059ACV9_EUCGR
LinkDB: A0A059ACV9_EUCGR
Original site: A0A059ACV9_EUCGR 
ID   A0A059ACV9_EUCGR        Unreviewed;      2289 AA.
AC   A0A059ACV9;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN   ORFNames=EUGRSUZ_J00810 {ECO:0000313|EMBL:KCW51230.1};
OS   Eucalyptus grandis (Flooded gum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX   NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW51230.1};
RN   [1] {ECO:0000313|EMBL:KCW51230.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW51230.1};
RA   Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT   "The genome of Eucalyptus grandis.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00000720};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
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DR   EMBL; KK198762; KCW51230.1; -; Genomic_DNA.
DR   STRING; 71139.A0A059ACV9; -.
DR   EnsemblPlants; KCW51230; KCW51230; EUGRSUZ_J00810.
DR   Gramene; KCW51230; KCW51230; EUGRSUZ_J00810.
DR   eggNOG; KOG3628; Eukaryota.
DR   InParanoid; A0A059ACV9; -.
DR   OMA; TGTCKEG; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd05931; FAAL; 1.
DR   Gene3D; 1.10.405.20; -; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.30.70.1990; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 2.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR036736; ACP-like_sf.
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; IPR018028; Catalase.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR020835; Catalase_sf.
DR   InterPro; IPR040097; FAAL/FAAC.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   PANTHER; PTHR22754:SF32; DISCO-INTERACTING PROTEIN 2; 1.
DR   PANTHER; PTHR22754; DISCO-INTERACTING PROTEIN 2 DIP2 -RELATED; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 3.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1205..1228
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1249..1277
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1446..1467
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1479..1500
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1512..1539
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2077..2102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2122..2142
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1097..1171
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1070..1090
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1885..1905
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2289 AA;  253243 MW;  34E20CBE64B397E8 CRC64;
     MDSQKSVEDQ FSKLHPCLPL DTRIGVVGGG PSGLSAAYAL AKLGYRDITV IEKHNTVGGM
     CESVEIEESG TQLEEMDLHK LALIDSLTGE YHDINVAEDY MSLVSLTLDI QDKAKDTNRI
     GIHAVSDIAS DLTPAYLEAH GIKSVPKSVQ YGYTASGYGF VQDMPYAYIH EFTRTSMAGK
     IRRMKGGYMN LWKKISDSLL IKVCCNTEVQ AVRRNGSGVN VDITNSSGET EHKEFDKIII
     SGAFPFKNSR TYRSTSSSTE AETGLLDVSD LERELFSKVQ TIDYYTTVLK IKGLERIPVG
     FYYLGEYMED PSTIGHPVAI QRFYADSNIF LFWSYGDSVN IRGSNVIDLA IEVVRRMGGQ
     VEKVFLQRRF KYFPHVSSKD MKEGFYERIE SELQGHRNTY YVGGLFAFEL TERNSSYAMA
     LICKHFASAN SLPALPYVKS LFTLQLDQEE TGLKTLSETH GIVFPDLPNL DSYLKHWAAK
     EITQNKTLYT WINEEGAVVC QRTYAELDSN ASCIAHKLLT SRKPTIKPGD RVLLVHVPGL
     DFVDSFFGCL RAKVVPVPVL PPDPLQRGGQ ALTKIENIAK LCNAVAILST VGYHSAVRAG
     SVKNLISFTR KSVESTAQWP NLPWLHTDSW IKSSKVLPAS NIGSQSESQP DDLCFLQFTS
     GSTGDAKGVM ITHGGLIHNV KLMRRRYRST SNTVLVSWLP QYHDMGLIGG LFTAMVCGGT
     AILFSPLTFI RNPLLWLQTI SDYKATHSAG PNFAFELVIR RLEADKAKAH DYDLSSMIFF
     MIAAEPVRQK TLKRFVELTR PYGLSQEVMA PGYGLAENCV FVGCAYGKKK PILVDWQGRI
     CCGYVDPNDA DVDIRIVDAD TGLEVDEDGK EGEIWISSPS AGIGYWGKEE LSQKTFRNKL
     QKYPGRKYTR TGDLGRVIQG NLFITGRIKD LIIVAGRNIY SADVEKTVES SSELLRPGCC
     AVISVPEDVL SAKGISLPDA SDEVGLVVIA ELKDGKPVDK DIIKQIESHV AEEHGVTVAS
     VKLIRPRTIS KTTSGKIKRF ECLKQFVDGT LNTVPDPIVT KRLLTRSFTT GTCREGNTPR
     SHLAKSSLPP SPKLSNRNIV EFLKQLVSEQ MGISIQNISA TESLVSYGID SIGVVRAAQK
     LSDFLGVPVG AVDIFTATCI ADLANFTENL LMKSQPHLVT TQSNHSEPEI LTADFSVEIS
     RLHPWLIWSF QLLALLYVSF ILVFPAYLSV SAFQILVVAS QKLIDGLPWL HHTSVVLLAP
     LFWILCIALT SISIAFFGNS FLRINYTLTP EVSVWSVDFV KWWALYKAQE VSSKVLAVHL
     RGTVFLKHWF EMLGARIGSS VLLDTVDITD PSLVSIGDGA VIAEGALLQS HEVRNSILRF
     QPIRIGRNCS VGPYAVIQKG SVLGEGAEVL SLQKSEGGKS ALKMAKAENI LKVSPGSLKE
     TIQQFMGIYM VGLVSSLSAA AVFLLYMRLS QKVPSLEQLA FLCISGALHW VPFTIVAYAT
     MFTNTLPNPF EFAISLATAY FAHGLVLSLL TSIFTNLLAS KEKKTQTHIK TWLGHRLAVA
     CHLRFAKLLS GTEAFCMYLR LLGAKVGKYC SIRSINPVTD PRMVSIGAGV HLGDFSRIMT
     GFYSQSGYIQ SNVHVKDNSV IGSQSLILPG SVVEKDVILG AISVAPVNSV LQSGGVYMGS
     QSPVMVKNTT HAMDDRIEEM DSRYKRIVGN LAANLAATTL KVKSRYFHRI GVSGKGYLKL
     YDDIQGLPEH NIFGPGKKYT VIVRHSNSLS ADDDARLDAR GAALRILSDE KGDDSPLLDL
     TLKTGKAFYA RTISDFATWL VCGLAAREEH VKRVPHVRDA VWTSLRQADS YAEMHYYSNI
     CRLFRFKDGQ EMYVKFKLRP SDKNIGEDTG KVEPSGILPP ETGAIPRDAN DTRPLLFLAE
     DFQNRVKSPN GVRYIFQLQV MPVPQDEAAR DIALDCTKPW DESQFPYIDV GEVIINENLT
     KEGSERLEFN PFLRCHEVDV IRATSSSQSA SIDHGRSLVY EICQHLRNGD PLPEAWRVFL
     EQSDVKVDLS GCPMAAALQR KDTEKVTLSR PWYLTTWAVF AQPLLQTILP YFLLGLIIYF
     PLNLLLHCKN TRNMPVHWTF PFFWVSTGVL AALACVAAKY ILVGKKREEE TVHIWSRGVF
     MDTVWQAIRT VFGDYFVEMT SGSALFLMWM KLMGSYIELD KGTYVDSMGA ALNPEMVEVE
     GGGSVEREAL LFGHVYDGEG GVVKFGKIVV GERGFVGSRA VAMPGVVVES EGSLSALSLA
     MKGEVIRSR
//
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