ID   CCL8_HUMLU              Reviewed;         607 AA.
AC   M4IS90;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=Probable CoA ligase CCL8 {ECO:0000305|PubMed:23300257};
DE            Short=HlCCL8 {ECO:0000303|PubMed:23300257};
DE            EC=6.2.1.- {ECO:0000305|PubMed:23300257};
GN   Name=CCL8 {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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, 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 {ECO:0000269|PubMed:23300257}.
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, flowers and cones. {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; JQ740210; AGA17925.1; -; mRNA.
DR   AlphaFoldDB; M4IS90; -.
DR   SMR; M4IS90; -.
DR   GO; GO:0005829; C:cytosol; IDA: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..607
FT                   /note="Probable CoA ligase CCL8"
FT                   /id="PRO_0000452953"
FT   REGION          305..391
FT                   /note="SBD1"
FT                   /evidence="ECO:0000250|UniProtKB:Q42524"
FT   REGION          392..453
FT                   /note="SBD2"
FT                   /evidence="ECO:0000250|UniProtKB:Q42524"
FT   BINDING         236..244
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q81G39"
FT   BINDING         391..396
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q81G39"
FT   BINDING         474
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q81G39"
FT   BINDING         486..489
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q81G39"
FT   BINDING         591
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q81G39"
SQ   SEQUENCE   607 AA;  66146 MW;  C455F764DEDA68DD CRC64;
     MHLNLKSLCS LTLISQAKTS NPFLSFSNCR PFSSLHSGSA NLILMELLKE VAKEGSSASV
     GVAIRADQKS YSYKQLISSA QRICSLLCST DLKASHKAGK QVTPALINGL SGHGHLGGAR
     VGIVAKPSAE FVTGVLGTWL SGGVAVPLAL SYPEAELLHV MTDSDISMIL STEDHQELMQ
     KIAAKTAAQF SLIPPVPSSC SQEGAVDHLQ TGDINTDSIL HNTEISNENP ALIVYTSGTT
     GKPKGVVHTH KSINAQVQTL AKAWEYTPAD QFLHCLPLHH VHGLFNALFA PLYARSTVEF
     MPKFSVRGIW QRWRESYPTC ETKVDDCITV FTGVPTMYTR LIQGYEAMDP ELKEASASAA
     KQLRLMMCGS SALPIPVMQQ WQTITGHRLL ERYGMTEFVM AISNPLKGER KAGTVGKPFP
     GVEVRIVAED ENGSDTTGVG ELCVRSPSLF KEYWRLPEVT KSSFTDDGFF KTGDAGKVDE
     DGYYVILGRT SADIMKVGGY KLSALEIESV LLEHPTVEEC CVLGLPDKDY GEAVSAIIVP
     AAEAKKKGEE ESKPAISLEE LFSWAQHKLA PYKLPTRLFL WDSLPRNAMG KVNKKELKKK
     LTVEQGV