ID   CCL5_HUMLU              Reviewed;         551 AA.
AC   M4IQR7;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 1.
DT   03-AUG-2022, entry version 21.
DE   RecName: Full=Probable CoA ligase CCL5 {ECO:0000305|PubMed:23300257};
DE            Short=HlCCL5 {ECO:0000303|PubMed:23300257};
DE            EC=6.2.1.- {ECO:0000305|PubMed:23300257};
GN   Name=CCL5 {ECO:0000303|PubMed:23300257};
OS   Humulus lupulus (European hop).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Cannabaceae; Humulus.
OX   NCBI_TaxID=3486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GENE
RP   FAMILY, AND NOMENCLATURE.
RC   STRAIN=cv. Nugget;
RX   PubMed=23300257; DOI=10.1093/mp/sst004;
RA   Xu H., Zhang F., Liu B., Huhman D.V., Sumner L.W., Dixon R.A., Wang G.;
RT   "Characterization of the formation of branched short-chain fatty acid:CoAs
RT   for bitter acid biosynthesis in hop glandular trichomes.";
RL   Mol. Plant 6:1301-1317(2013).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:M4IRL4}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed at low levels in glandular
CC       trichomes (lupulin glands) after flowering, and, to a lower extent, in
CC       stems, leaves, cones and flowers. {ECO:0000269|PubMed:23300257}.
CC   -!- DEVELOPMENTAL STAGE: Accumulates progressively in glandular trichomes
CC       (lupulin glands) after flowering. {ECO:0000269|PubMed:23300257}.
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. {ECO:0000250|UniProtKB:Q42524}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; JQ740207; AGA17922.1; -; mRNA.
DR   AlphaFoldDB; M4IQR7; -.
DR   SMR; M4IQR7; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016405; F:CoA-ligase activity; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding.
FT   CHAIN           1..551
FT                   /note="Probable CoA ligase CCL5"
FT                   /id="PRO_0000452950"
FT   REGION          274..345
FT                   /note="SBD1"
FT                   /evidence="ECO:0000250|UniProtKB:Q42524"
FT   REGION          346..410
FT                   /note="SBD2"
FT                   /evidence="ECO:0000250|UniProtKB:Q42524"
FT   BINDING         204..212
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q81G39"
FT   BINDING         345..350
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q81G39"
FT   BINDING         431
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q81G39"
FT   BINDING         443..446
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q81G39"
FT   BINDING         537
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q81G39"
SQ   SEQUENCE   551 AA;  60044 MW;  82B8EC368CB8DB70 CRC64;
     MENSSKAIVD ERSGYCKSNS IFYSKREPVQ LPQNHSVDVT TFISSRAHHG KIAFIDAATG
     RHLTFPQLWR AVDSVATCLS AMGIRKGDVI LLLSPNSIYF PVVCLAVMSL GAIITTTNPL
     NTPREIAKQI TDSKPVLAFT IPQLVSKIAG SNLPIVIIDD EVKSSLEKTL NIVSSLGEMM
     RKEPSPNRIG YRVNQEDTAT LLYSSGTTGA SKGVVSSHKN LIAMVQTILS RFGTEDGEHT
     FICTVPMFHI YGLAAFAMGL LSSGSTIVIL SKFEIHEMLS AIEKYRATYL PLVPPILMAL
     LKNANHIRAK YDLSSLQSVL SGGAPLSKEV IEGFVENYPT VSILQGYGLT ESTGIGASTD
     CLQESRRYGT AGMLSPSMEA KIVNPETGEA LSVNRTGELW LRGPTIMKGY FSNEEATSST
     IDSEGWLRTG DLCYIDEDGF IFVVDRLKEL IKYKGYQVAP AELEALLLSH PEISDAAVIP
     YPDKEAGQFP MAYVVRKGGS NLSESTVMDF IAKLVAPYKR IRKVAFVASI PKNPSGKILR
     KDLIKLATSK L