CCL10_HUMLU
ID CCL10_HUMLU Reviewed; 543 AA.
AC M4IQS1;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Probable CoA ligase CCL10 {ECO:0000305|PubMed:23300257};
DE Short=HlCCL10 {ECO:0000303|PubMed:23300257};
DE EC=6.2.1.- {ECO:0000305|PubMed:23300257};
GN Name=CCL10 {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], GENE 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 -!- 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; JQ740212; AGA17927.1; -; mRNA.
DR AlphaFoldDB; M4IQS1; -.
DR SMR; M4IQS1; -.
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..543
FT /note="Probable CoA ligase CCL10"
FT /id="PRO_0000452955"
FT REGION 267..337
FT /note="SBD1"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT REGION 338..402
FT /note="SBD2"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT BINDING 196..204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
FT BINDING 337..342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
FT BINDING 423
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
FT BINDING 435..438
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
FT BINDING 529
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q81G39"
SQ SEQUENCE 543 AA; 60208 MW; 6687F32991CA72FB CRC64;
MEKCFNPETQ IYSSHRPPVN FPTDPKLSLT SFLFRSSASY PNRTALIDAD SGQTLTFLKL
KTQVSKLAHS LVQLNIKKND VVLIFAPNSI HFPVCFFSIA ALGAITTTCN PSYTFTELSN
QAKDCNPTLV ITVPELWEKA RKLNLPAIIL PSPSNSKLSS KSEFWFFSDL TRKSDRFSEL
PISDVRQSDV AALLYSSGTT GKSKGVVLSH KNFITTSLMV TSDQDRYGDP QNICMCFLPM
FHIFGLSVIA YSQLRRGNGV VSMGKFELEG ALRAVEMYRV THLFVVPPVM IALAKESVVV
RRYDLSSVKE ILSGAAPLGK NVMEQCARNV PGAAIIQGYG MTETCGIISI EDSKKGCRFS
GSTGMLAPGI ESQIMDTKRW NPLPPNQEGE IWLRGPNMMQ GYLNNLEATK STIDEQGWVK
TGDIGYFDEE GQLFVVDRLK ELIKCYGFQV APAELEALLL SHPEILDAVV IPFPDEKAGE
VPIANVVRSP NSSLSEEDVQ RFIEKQVAPF KKLRRVTFVS SVLKSPAGKI LRRELIQKVR
SKI