ID   A0A1A9WTD0_9MUSC        Unreviewed;       442 AA.
AC   A0A1A9WTD0;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   03-MAY-2023, entry version 30.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:GBRI031262-PA};
OS   Glossina brevipalpis.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC   Glossinidae; Glossina.
OX   NCBI_TaxID=37001 {ECO:0000313|EnsemblMetazoa:GBRI031262-PA, ECO:0000313|Proteomes:UP000091820};
RN   [1] {ECO:0000313|Proteomes:UP000091820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAEA {ECO:0000313|Proteomes:UP000091820};
RA   Aksoy S., Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:GBRI031262-PA}
RP   IDENTIFICATION.
RC   STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GBRI031262-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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DR   AlphaFoldDB; A0A1A9WTD0; -.
DR   STRING; 37001.A0A1A9WTD0; -.
DR   EnsemblMetazoa; GBRI031262-RA; GBRI031262-PA; GBRI031262.
DR   VEuPathDB; VectorBase:GBRI031262; -.
DR   OrthoDB; 1365844at2759; -.
DR   Proteomes; UP000091820; Unassembled WGS sequence.
DR   GO; GO:0047710; F:bis(5'-adenosyl)-triphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   CDD; cd01275; FHIT; 1.
DR   CDD; cd07572; nit; 1.
DR   Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 1.
DR   Gene3D; 3.30.428.10; HIT-like; 1.
DR   InterPro; IPR003010; C-N_Hydrolase.
DR   InterPro; IPR036526; C-N_Hydrolase_sf.
DR   InterPro; IPR039383; FHIT.
DR   InterPro; IPR019808; Histidine_triad_CS.
DR   InterPro; IPR011146; HIT-like.
DR   InterPro; IPR036265; HIT-like_sf.
DR   InterPro; IPR045254; Nit1/2_C-N_Hydrolase.
DR   InterPro; IPR001110; UPF0012_CS.
DR   PANTHER; PTHR23088:SF27; DEAMINATED GLUTATHIONE AMIDASE; 1.
DR   PANTHER; PTHR23088; NITRILASE-RELATED; 1.
DR   Pfam; PF00795; CN_hydrolase; 1.
DR   Pfam; PF01230; HIT; 1.
DR   SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1.
DR   SUPFAM; SSF54197; HIT-like; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
DR   PROSITE; PS00892; HIT_1; 1.
DR   PROSITE; PS51084; HIT_2; 1.
DR   PROSITE; PS01227; UPF0012; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          8..261
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS50263"
FT   DOMAIN          296..404
FT                   /note="HIT"
FT                   /evidence="ECO:0000259|PROSITE:PS51084"
FT   MOTIF           389..393
FT                   /note="Histidine triad motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00464"
FT   ACT_SITE        391
FT                   /note="Tele-AMP-histidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-1"
FT   BINDING         322
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT   BINDING         378
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT   BINDING         384..387
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT   BINDING         393
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT   SITE            409
FT                   /note="Important for induction of apoptosis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639383-3"
SQ   SEQUENCE   442 AA;  50743 MW;  32AE78F1ED9DCD30 CRC64;
     MSSTRTKPLV AVTQMCSTSN KAENMRQVEK LIEMAKAQSA EFVFLPECCD FVGENRQQTL
     ELSEPLTGPT IEQYQGLAQK HDIWLSLGGF HESILDEYER KTDKIYNAHV ILNNCGELIA
     VYRKLHLFDV DTPEFKFQES KIVCGGQHLV SPIETPIGNL ALQICYDMRF PETSILLRRS
     GAQLLTYPSA FTYYTGKAHW EILLRSRAIE TQCFIIAAAQ MGSHNPKRRS WGHALIIDPW
     GKILADLGEK ELDVATVEID LDSLEPMRCR MPCFNHRRDD IYSLVAYGEG TIECQTDYMF
     AENCIKKETI FFESPYSYAF TNICCVVEGH VLVSTKRIVP RLKDLNSAEI SDLFNVTCRI
     QRMLENFYKT TASTVNVQDG PLAGQTVPHV HFHVMPRRQG DFEHNDEVYR MLEIVNKKKQ
     RSIEERINEA QSYREALRNM KQ
//