ID   A0A195BD00_9HYME        Unreviewed;      1415 AA.
AC   A0A195BD00;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=phospholipase A1 {ECO:0000256|ARBA:ARBA00013179};
DE            EC=3.1.1.32 {ECO:0000256|ARBA:ARBA00013179};
GN   ORFNames=ALC53_07494 {ECO:0000313|EMBL:KYM82087.1};
OS   Atta colombica.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Atta.
OX   NCBI_TaxID=520822 {ECO:0000313|EMBL:KYM82087.1, ECO:0000313|Proteomes:UP000078540};
RN   [1] {ECO:0000313|EMBL:KYM82087.1, ECO:0000313|Proteomes:UP000078540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Treedump-2 {ECO:0000313|EMBL:KYM82087.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYM82087.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Atta colombica WGS genome.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC         glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32;
CC         Evidence={ECO:0000256|ARBA:ARBA00000111};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000256|ARBA:ARBA00010701}.
CC   -!- SIMILARITY: Belongs to the exosome component 10/RRP6 family.
CC       {ECO:0000256|ARBA:ARBA00043957}.
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DR   EMBL; KQ976522; KYM82087.1; -; Genomic_DNA.
DR   STRING; 520822.A0A195BD00; -.
DR   Proteomes; UP000078540; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0000176; C:nuclear exosome (RNase complex); IEA:InterPro.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008970; F:phospholipase A1 activity; IEA:UniProtKB-EC.
DR   GO; GO:0000467; P:exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   CDD; cd00707; Pancreat_lipase_like; 1.
DR   CDD; cd06147; Rrp6p_like_exo; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 1.10.150.80; HRDC domain; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR012588; Exosome-assoc_fac_Rrp6_N.
DR   InterPro; IPR010997; HRDC-like_sf.
DR   InterPro; IPR002121; HRDC_dom.
DR   InterPro; IPR044876; HRDC_dom_sf.
DR   InterPro; IPR013818; Lipase.
DR   InterPro; IPR033906; Lipase_N.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR045092; Rrp6-like.
DR   InterPro; IPR049559; Rrp6p-like_exo.
DR   InterPro; IPR000734; TAG_lipase.
DR   PANTHER; PTHR12124:SF47; EXOSOME COMPONENT 10; 1.
DR   PANTHER; PTHR12124; POLYMYOSITIS/SCLERODERMA AUTOANTIGEN-RELATED; 1.
DR   Pfam; PF01612; DNA_pol_A_exo1; 1.
DR   Pfam; PF00570; HRDC; 1.
DR   Pfam; PF00151; Lipase; 1.
DR   Pfam; PF08066; PMC2NT; 1.
DR   PRINTS; PR00821; TAGLIPASE.
DR   SMART; SM00474; 35EXOc; 1.
DR   SMART; SM00341; HRDC; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF47819; HRDC-like; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50967; HRDC; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Exosome {ECO:0000256|ARBA:ARBA00022835};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078540};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          596..676
FT                   /note="HRDC"
FT                   /evidence="ECO:0000259|PROSITE:PS50967"
FT   REGION          1..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          786..815
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          861..896
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          928..948
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..36
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..65
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        786..811
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        875..892
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1415 AA;  162838 MW;  95EE81E8307FE245 CRC64;
     MTAAKDGYNH LNLTLRNEES ESEEMKRKRE RENVTDSVFP LHFVEYSSRD IEEEDDDEDD
     DDDNDTAHGS NTAISSLFTN FGRECWKTRN QRIMDDSPPH VAPEGEDDFE IQSSAHVTNM
     KHVELAENWD YEANVSQNND IEVEKKDEPS IRLPGYATFE DYIQDAFDAM RAGIKAANNL
     PAGDNFNYYA CFPSFNDARQ KDKERILDTM QSIIKLAGGS GNIQNRDIDE KFDLLLEAND
     QLLDQANILM DEESGILRNP QVELVVSQMP KPVVNGTWNI KTNTNQISDN LEKVRLLGGK
     NIQRPQLMFK DKIDNSSKPW MPRIKDKPNS LKPLALHVEE NEHGEVFNHP YEFELDKFET
     PECQLKKRIP VEYKSLDDTN FVFIDKPADI NILLEDLRNH KEIAVDLEHH SYRTFQGITC
     LMQISTIQTD YLIDTLSLRS ELYQLNEIFT KPSILKVFHG ADMDILWLQR DLSLYVVNMF
     DTHQAAKQLN LPYLSLAYLL NKYCEIDPNK HFQLADWRIR PLPVELMKYA REDTHYLLYV
     KDMLKNELID AANGKSNILK AVYDQSTEIC KRTYVKPIWT EESCMNMYRK SQKSFNNKQM
     YALMELHRWR DLTARQEDDS IGYILPNHML LNIAETLPRE MQGILACCNP IPPLVRQNLL
     KIHKIILKAR EQPLVKSIAE QDIRQRPTQQ NHMDTGASLY IPHDVPSGTE ARADLPCLLN
     KNIVRSELSE ANKCQTTKHT ITIFDSSDLS EDEETKDSKN GNKKKIIFIS PFMRYRCVIP
     MVMDQEAKER EKEQQKKEET EKEEKTLKSQ NECINEAEIN ESKNRVYEHF KQMSQKNIQA
     EVQLKKKKKS DNIFLNLTRR QRKRKFDTGN ESQRKNDAND FSTSTSHLNS ETIHVSKKAK
     QKTLKVIEEQ KLQESLAQVQ SDNRNSVTIK SIRARKKGDK KANEEMLRKQ GLLPSTKFDY
     KSVDFSSFQG GSTQSSANRT QFQQPRVSKY FVMAYLTKWD DKYFIYTCIL KDNISKANVL
     VDDHDGICNH PFEHALNETT FVTTLSLFNE TTTLTNFTYT LSTSNSRELF SDSRQVDCFG
     LGKKVAAALE WFFSSKPNGS DALDVQFLLS SRKQPHRVQV VLGEQFGLEW TDFKIERRTV
     VIIHGFLSHG QETWIRDMEK ALLEWGDVNV VIIDWSAGSN TWNYYKAAVN TRIVGYQLSK
     FIEHVTNATI AQSGVNNWGP LHLVGHSLGA HICGFAAREL KKRQNKWTVQ RITGLDPAQP
     CFRKADTSVH LHKNDAPFVD VIHTNGRLLT NLGLGLPEAI GHVDFYPNGG KTQPGCVRTS
     YFDYLPIPTA AIQRAICSHG RSYVYLTESL TSVTARNCSF WAHQWNLTYR HFLQIIAEPC
     DENICSEMGI RAEMYNQRGS FFVATASTSP FCGVL
//