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Database: UniProt
Entry: A0A182LYC2_9DIPT
LinkDB: A0A182LYC2_9DIPT
Original site: A0A182LYC2_9DIPT 
ID   A0A182LYC2_9DIPT        Unreviewed;       403 AA.
AC   A0A182LYC2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=5' exonuclease Apollo {ECO:0000256|ARBA:ARBA00039555};
DE            EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
DE   AltName: Full=DNA cross-link repair 1B protein {ECO:0000256|ARBA:ARBA00041693};
DE   AltName: Full=SNM1 homolog B {ECO:0000256|ARBA:ARBA00042738};
OS   Anopheles culicifacies.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles; culicifacies species complex.
OX   NCBI_TaxID=139723 {ECO:0000313|EnsemblMetazoa:ACUA004919-PA, ECO:0000313|Proteomes:UP000075883};
RN   [1] {ECO:0000313|Proteomes:UP000075883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A-37 {ECO:0000313|Proteomes:UP000075883};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles culicifacies species A.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:ACUA004919-PA}
RP   IDENTIFICATION.
RC   STRAIN=A-37 {ECO:0000313|EnsemblMetazoa:ACUA004919-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC         Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC         ChEBI:CHEBI:140347; EC=3.5.2.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00001526};
CC   -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC       {ECO:0000256|ARBA:ARBA00004574}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase (DRMBL)
CC       family. {ECO:0000256|ARBA:ARBA00010304}.
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DR   EMBL; AXCM01001777; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A182LYC2; -.
DR   STRING; 139723.A0A182LYC2; -.
DR   EnsemblMetazoa; ACUA004919-RA; ACUA004919-PA; ACUA004919.
DR   VEuPathDB; VectorBase:ACUA004919; -.
DR   OrthoDB; 23465at2759; -.
DR   Proteomes; UP000075883; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006396; P:RNA processing; IEA:UniProt.
DR   Gene3D; 3.40.50.12650; -; 1.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR   InterPro; IPR011084; DRMBL.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   PANTHER; PTHR23240:SF8; 5' EXONUCLEASE APOLLO; 1.
DR   PANTHER; PTHR23240; DNA CROSS-LINK REPAIR PROTEIN PSO2/SNM1-RELATED; 1.
DR   Pfam; PF07522; DRMBL; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE   3: Inferred from homology;
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Telomere {ECO:0000256|ARBA:ARBA00022895}.
FT   DOMAIN          229..316
FT                   /note="DNA repair metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|Pfam:PF07522"
FT   REGION          371..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..395
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   403 AA;  46713 MW;  220FBC4D47C575E9 CRC64;
     MSTFPGYIPE LPGIAIDRFD QPVRDRAKVF FLSHCHMDHM HGLAPNQPLL GTLYMSPHSA
     VIIGLRYPKQ TVYRMPIREQ LTLSITAPTG ESTYELCVRT VPAEHCPGSV MFYFETKTVR
     LLYTGDFRLS TESMAVIEQD NIRPEIVYLD TTFLDREYAY FPTRKQSMDR IIELCSQWLD
     ADQRNIVSLW PPATYGSEEL FHQLYSHLQQ RIHIYSSQRE TYNHFDILKD VFTDDPVGAR
     IHACNGKTLQ GEMSCRKLDA NTKYVMTIRP SARKWRNLQR DEPFWMEGNK NLWFVCYSSH
     ASSSELVEFI RTLQPEARDI RFNVVEDETD RSRKEQYLQA LLSPEDGSMD DEVNSESEEM
     YILPDYDFGA STSTQHATNE WARSDSEDDA SMKTPPSKLA KRC
//
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