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4CLL8_ORYSJ
ID   4CLL8_ORYSJ             Reviewed;         609 AA.
AC   Q8GVF9;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Putative 4-coumarate--CoA ligase-like 8;
DE            EC=6.2.1.-;
GN   Name=4CLL8; OrderedLocusNames=Os07g0639100, LOC_Os07g44560;
GN   ORFNames=OJ1340_C08.126;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [3]
RP   GENE FAMILY.
RX   PubMed=18627494; DOI=10.1111/j.1469-8137.2008.02534.x;
RA   de Azevedo Souza C., Barbazuk B., Ralph S.G., Bohlmann J., Hamberger B.,
RA   Douglas C.J.;
RT   "Genome-wide analysis of a land plant-specific acyl:coenzyme A synthetase
RT   (ACS) gene family in Arabidopsis, poplar, rice and Physcomitrella.";
RL   New Phytol. 179:987-1003(2008).
CC   -!- DOMAIN: Both substrate-binding domains (SBD1 and SBD2) are involved in
CC       the substrate recognition, and are sufficient to confer the substrate
CC       specificity.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AP005292; BAC45208.1; -; Genomic_DNA.
DR   EMBL; AP014963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; Q8GVF9; -.
DR   SMR; Q8GVF9; -.
DR   STRING; 4530.OS07T0639100-00; -.
DR   PaxDb; Q8GVF9; -.
DR   PRIDE; Q8GVF9; -.
DR   eggNOG; KOG1176; Eukaryota.
DR   InParanoid; Q8GVF9; -.
DR   Proteomes; UP000000763; Chromosome 7.
DR   Proteomes; UP000059680; Chromosome 7.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR   GO; GO:0016207; F:4-coumarate-CoA ligase activity; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016405; F:CoA-ligase activity; IBA:GO_Central.
DR   GO; GO:0106290; F:trans-cinnamate-CoA ligase activity; IEA:UniProt.
DR   GO; GO:0009698; P:phenylpropanoid metabolic process; IEA:UniProt.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
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.
DR   InterPro; IPR042099; ANL_N_sf.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..609
FT                   /note="Putative 4-coumarate--CoA ligase-like 8"
FT                   /id="PRO_0000351634"
FT   REGION          276..348
FT                   /note="SBD1"
FT   REGION          349..450
FT                   /note="SBD2"
FT   BINDING         194..202
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         349..354
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         482
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         497
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         589
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   609 AA;  64509 MW;  75FE211B56CA8557 CRC64;
     METELHLAAG YCAATGVYRS GHPPQFAAAA ALSFPEYILP HMLLPGRRAR PAFVDASTGA
     ALSFAGLRAL SLRVARALAA AGLRRGRVAL LLSPNSLHFP ALSLAVLSLG AVLSAANPLL
     TPDELARQAD DAKPFLALVT GELAPKLRSI APDVKLVLVE QLLADVAAEV DDDETLDLPA
     ANIGRDDAAL LFYSSGTTGR SKGVVSTHGN AIAMAASLER AWGGGGGGGE KPQQYDDHDE
     AYGCVLPMFH MFGFSSFVMG TAALGATAVV VPGRFSVEKT MAAVEEYGVT RLLVVPPMVV
     KMVAAAAGDG EPSRRRLRLR QVVSSGAPLQ REHMARFRSC FPAVNLGQCY GLTETTGIVT
     MCDLQHNDNG IDKVEMPPSS TDMTFVAVAA TTTEVKERST GGGGGGGGVS IGRLMPDVEA
     KIVDPDSGEL LPPRRTGELW VRGPSTMRGY LNNEEATALA LVAAAGSVSV SGGGERWLRT
     GDLCYVDSRG LVYVVDRVKE LIKCNAYQVA PAELEDVLAT HPDIHDAAVA PYPDKEAGEI
     PMAYVVKKQG SGHLQEDEVI SFVQNKVAPY KKIRKVVFVD SIPRSPSGKI LRRQLKNLLQ
     GSILHRSRM
 
 
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