ID A0A0V0ZH31_9BILA Unreviewed; 550 AA.
AC A0A0V0ZH31;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Snake venom 5'-nucleotidase {ECO:0000313|EMBL:KRY11817.1};
GN ORFNames=T12_10498 {ECO:0000313|EMBL:KRY11817.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY11817.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY11817.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY11817.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC {ECO:0000256|ARBA:ARBA00006654, ECO:0000256|RuleBase:RU362119}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRY11817.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDQ01000182; KRY11817.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0ZH31; -.
DR STRING; 990121.A0A0V0ZH31; -.
DR Proteomes; UP000054783; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008252; F:nucleotidase activity; IEA:UniProt.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR CDD; cd07409; MPP_CD73_N; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 1.
DR InterPro; IPR008334; 5'-Nucleotdase_C.
DR InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR InterPro; IPR006146; 5'-Nucleotdase_CS.
DR InterPro; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR PANTHER; PTHR11575:SF24; 5'-NUCLEOTIDASE; 1.
DR PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1.
DR Pfam; PF02872; 5_nucleotid_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1.
DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362119};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362119};
KW Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW Signal {ECO:0000256|RuleBase:RU362119}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT CHAIN 22..550
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT /id="PRO_5006773773"
FT DOMAIN 25..238
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 332..512
FT /note="5'-Nucleotidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02872"
SQ SEQUENCE 550 AA; 62170 MW; 4C4ADF6010C52B21 CRC64;
MVCQTNKHWF LSLIFCWTAQ SLKLTILHTN DVHARFTPFN NDLKDCSASD IEANECFGGA
AKRMTAVTRI REEEENVLLF DAGDQYQGTL WYVLFRHQAV VEVMNAIGYD AMALGNHEFD
HALAGLIPLL REAKFPIMAA NLVSDNEKVK TLVKPYTIFT FDDVKVGVIG YVTPLTKRLS
KAHEVEFEDE IQVLTRIAAQ LKEEGVNMII AVGHSGIQMD RLICQKVPNI DIVVGGHTNT
FLYSGKPPSV EEIQGPYPEI YNDQGKPCLV VTDYAFGKYL GFLKVEYDKE LDRVTKWDGN
PILLDNRFHA SREMENILAT YKHQLHEFTS TVIGSTAVKI DGRFSTCRLQ ECNLGNMLTD
HLVRKVMKES DIRLTENADS WAPAPIALIN SGGIRNYLKR YSGNVTLEDA YSIMPFGTQF
KLLEVTGPQL MEVFENSVSQ YWPDGPWGRF LQMSGARVAY NLSMPVGSRV HSLQLRCADC
PIPIYKNWDP EESYRLLIST FMANGGDDFS VFPNVPNHKL LNFTDTELVI DFFRTSSPVW
TGVEGRIIFI
//
