ID A0A0L7RA16_9HYME Unreviewed; 654 AA.
AC A0A0L7RA16;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Laccase-4 {ECO:0000313|EMBL:KOC67679.1};
GN ORFNames=WH47_11427 {ECO:0000313|EMBL:KOC67679.1};
OS Habropoda laboriosa.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Habropoda.
OX NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC67679.1, ECO:0000313|Proteomes:UP000053825};
RN [1] {ECO:0000313|EMBL:KOC67679.1, ECO:0000313|Proteomes:UP000053825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0110345459 {ECO:0000313|EMBL:KOC67679.1};
RA Pan H., Kapheim K.;
RT "The genome of Habropoda laboriosa.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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DR EMBL; KQ414620; KOC67679.1; -; Genomic_DNA.
DR RefSeq; XP_017787580.1; XM_017932091.1.
DR AlphaFoldDB; A0A0L7RA16; -.
DR STRING; 597456.A0A0L7RA16; -.
DR EnsemblMetazoa; XM_017932091.1; XP_017787580.1; LOC108570259.
DR GeneID; 108570259; -.
DR OrthoDB; 537265at2759; -.
DR Proteomes; UP000053825; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd13858; CuRO_1_tcLCC2_insect_like; 1.
DR CDD; cd13884; CuRO_2_tcLCC_insect_like; 1.
DR CDD; cd13905; CuRO_3_tcLLC2_insect_like; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR001117; Cu-oxidase_2nd.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709:SF532; L-ASCORBATE OXIDASE-LIKE PROTEIN; 1.
DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; Cupredoxins; 3.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000053825}.
FT DOMAIN 93..201
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 240..360
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 509..621
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT REGION 461..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 654 AA; 72448 MW; B26E45BC333E8C3D CRC64;
MRSTKNSDYM MMLATYGLRF LVVVFMIAAA ATFLHVNNYR PKQIFLSCDR PCHHLDWPMI
CRLKLTLEVF QSLSKSCGDC PQNETACLTK HCVSADGHRR GILTANRQLP GPTIQVCEND
ILVVDVINRL PGKAAAVHWR GQSQIESPYM DGAPLVTQCP IPSYTTFQYK FRASVAGTHL
WHSHAGADVS NGVFGALIVK QADIRDPHRP LYDIDDPNHV VLLSHWQHLP EIALTEGHVK
PAILLVNGRG RQSNGPNVPY TRFTVIPGRR HRFRVANAGG AGTCPITISI DAHPILLIAL
DGHPVEPRQV TSITLAKGER ADFILKANKA IASYWMNLHT SKECGTKPIN GAAILRYKGS
TTKEPQSVTE TTDQLEVEES MRRLAMTTNP AEKCGNPENL CVTEIQSLRK MPTVLRAPKT
DVTIRLPINY KMQTNDIVGN SGAEMRILNV NNVTFTYPSS PLLTQGTDVT EETLCSSTSD
DNDDARNENN ETASLSSRRC RRGDGLASDT CECVHVRYVP LGATVEIILL DQGGFDDLVY
HLHGYSFYVV GARKFGRSLP LQELKDLDEK GQLFPRNLDC TVAKDTVVVP KFGAVALRFK
ADNPGYWMLR DEHAAEWTRG LDVVLQVGET SDMVPAPQDF PKCGSFVGPD YFLI
//
