ID A0A151WTL4_9HYME Unreviewed; 703 AA.
AC A0A151WTL4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Cytosolic purine 5'-nucleotidase {ECO:0000313|EMBL:KYQ51107.1};
DE Flags: Fragment;
GN ORFNames=ALC60_09754 {ECO:0000313|EMBL:KYQ51107.1};
OS Trachymyrmex zeteki.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ51107.1, ECO:0000313|Proteomes:UP000075809};
RN [1] {ECO:0000313|EMBL:KYQ51107.1, ECO:0000313|Proteomes:UP000075809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ51107.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ51107.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex zeteki WGS genome.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family.
CC {ECO:0000256|ARBA:ARBA00009589}.
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DR EMBL; KQ982757; KYQ51107.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151WTL4; -.
DR STRING; 64791.A0A151WTL4; -.
DR Proteomes; UP000075809; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd07522; HAD_cN-II; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR008380; HAD-SF_hydro_IG_5-nucl.
DR InterPro; IPR023214; HAD_sf.
DR NCBIfam; TIGR02244; HAD-IG-Ncltidse; 1.
DR PANTHER; PTHR12103; 5'-NUCLEOTIDASE DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR12103:SF15; CYTOSOLIC PURINE 5'-NUCLEOTIDASE; 1.
DR Pfam; PF05761; 5_nucleotid; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000075809}.
FT REGION 62..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KYQ51107.1"
SQ SEQUENCE 703 AA; 81186 MW; F3F2859160F79203 CRC64;
LGLIVDYPKP GYGSTNDENT ARRFFENSSI SATITDVSEC LILRENAREK IPLIMELENC
NAHGDQDNTG PNTPQNDNDP SGNKKWYRQA SQRRHEFHGA GPRVRFPDDS NVFPEESIHR
TMFGLNVGLT RNDRSEQDLD SYNEGTHGAR SDKRELGHRI FVNRSLHLEN IKFYGFDMDY
TLAEYKSPQY EQLGFNLLKD RLVSLGYPQE IKAFEYDPSF PVRGLWFDTL HGNLLKVDAY
GNILVCVHGF EFLKHSQVYE LYPNKFLQLD ESRVYVLNTL FNLPETYLLA CLIDFFTNSP
QYTRERTGVK EGELTMSFKS IFQDVRNAVD WIHLHGDLKS KTIENLDEYV KKDERLPMFL
TRIRESGAKL FLLTNSDYVF TDKIMTYLFD FPHGARPDEP HRNWKTYFDT IVVDARKPLF
FGEGTILRQV DTKTGALKLG THKGPLHTGE VYSGGSCDVF TELIGAKGKD VLYVGDHIFG
DILKSKKIRG WRTFLIVPEL VQELHVWTDK CQLFAELQSL DVMLGEMYKN LDSSTKEKPD
ISKLRASIRD VTHKMDLAYG MMGSLFRSGS RQTFFSSQVV RYADLYAATF LNLIYYPFSY
MFRAPAMLMP HESTVAHEQR FVMETPMISR SRTFKLADEE EEHNRPSSKN LYVDHFNNQI
PHARPETPRN VTHTHDEDCS DEDSDSQKQA NQMRVSTRNI NCN
//