ID A0A0V0V7C7_9BILA Unreviewed; 1158 AA.
AC A0A0V0V7C7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Cytosolic purine 5'-nucleotidase {ECO:0000313|EMBL:KRX59400.1};
DE Flags: Fragment;
GN ORFNames=T09_10516 {ECO:0000313|EMBL:KRX59400.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX59400.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX59400.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX59400.1};
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'(3')-deoxyribonucleotidase family.
CC {ECO:0000256|ARBA:ARBA00009589}.
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:KRX59400.1}.
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DR EMBL; JYDN01000073; KRX59400.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0V7C7; -.
DR Proteomes; UP000054681; 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 GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR CDD; cd07522; HAD_cN-II; 1.
DR CDD; cd09337; LIM2_Paxillin_like; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 2.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 1.
DR HAMAP; MF_01988; Succ_CoA_alpha; 1.
DR InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR005810; CoA_lig_alpha.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR008380; HAD-SF_hydro_IG_5-nucl.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR005811; SUCC_ACL_C.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR InterPro; IPR001781; Znf_LIM.
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 Pfam; PF02629; CoA_binding; 1.
DR Pfam; PF00549; Ligase_CoA; 1.
DR Pfam; PF00412; LIM; 2.
DR SMART; SM00881; CoA_binding; 1.
DR SMART; SM00132; LIM; 2.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 2.
DR PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW ProRule:PRU00125}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00125}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 733..792
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 793..851
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX59400.1"
SQ SEQUENCE 1158 AA; 130517 MW; 9E8E3E1F1F2338E9 CRC64;
LGIFKSVAME NTMVKKYHRD PGKRVFVNRS LELEKIKFFG FDMDYTLAVY KSPEYEILGF
RLVIERLISI GYSPELLQLK YDNTFPIRGL WFDNLYGNLL KVDAFGNILV GVHGFEQAIE
SLYPNKFIQL SEDRVYVLNT LFNVPETYLI ACLVNYMDNC PGSSREPSGV KLGDMYMSYK
SMYQDVRAAV DWVHYHGDMK RITLNNLEKY VHKDPRLPML LTRMRDNGAK TFLLTNSGYF
YTDKVMTYLL DSETKSWRSY FDFIVVDANK PLWFAEGTVF RQVDQGTGTL RIGSHLGPLR
PNQIYAGGSS EVFSKLVGAR GREVLYLGDH IFGDVLRSKK GRGWRTFLVV PELVQELHVW
TERRGLFTRL QNLDIQLGAA FKNMDSSSEI RPDIREIRES MRSVTHEMDM AYGMLGSLFR
SGSRQTFFAS QVERYADLYA HSCCNLLYYP FFYFFRAPSM LMPHESTVEH EETGPIDFSG
LTPIDRGRNV TISESMEGLS VGEPMTTVHH HHPHHHHLQS CAVMNDSESK RFTRAETPTE
STYVHEEEER EEDSCVNNGN FSLVHDATQQ SAAAAAAATT TTTMQSQRMC KHALLVVVAA
WEKLHAPIDF HFWNKRRKEK QLAAANNKQW RLRKSMIIKP LSKEAFVLLR YSTLFSLLFI
TKQQLTALFA FSWDAFLSPH SVHSVEGTNS PMFGSFKRAK HVRIDFNDSM TNSNSDSIQN
DLARYGINNV SNEECEACKK SIVGQVAIAL GKMWHEEHFV CAHCGERLAH RNFYERSGSI
YCEHDYHRLF SPRCAYCNTP IKEKCITALD QTWHPEHFYC AKCGRPIGEE IFHEKDGRAF
CHKDYFTNFT PTCHGCKRPI TGHYITALNL IPRETRKFLK IGHETKVICQ GFTGKQATFH
CRQMLDYGTK IVGGVSPTKA GTKHLNLPVF GSVEEAVKET EADATILYVP AQASADAIHE
AIDAKVPLIV VITEGIPQLD MVKVKQKLLK QSDCRLVGPN CPGLIRPNEC KIGIMPGHIH
QPGCVGIVSR SGTLTYEAVQ QTTDVGLGQT LCIGIGIILI GEIGGNAEER AAEYLKINNT
GANAKPVVSF IAGVTAPPGR RMGHAGAIIS GGKGTAAHKI EALKEAGVTV VMSPAQMGIS
LARHFDLAHS NELNDIYF
//
